DOCSLIB.ORG

In the at Same Body We

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
In the at Same Body We 375 Effects of Nutritional Level on Digestive Enzyme Activities in the Pancreas and Small Intestine of Calves Slaughtered at Same Body We坷ht X. B. Wang, T. Ogawa, S. Suda, K. Taniguchi1, H. Uike2, H. Kumagai2 and K. Mitani Faculty of Applied Biological Science, Hiroshima University, Higashi-hiroshima 739, Japan ABSTRACT : Six Holstein heifer calves weaned at 45 whole pancreas were higher (p < 0.05) in HDG calves. dayspBa응 e were randomly allocated into high daily gain Disaccharidase activity of the whole small intestinal (1.1 kg/d, HDG) and low daily gain (0.56 kg/d, LDG) mucosa was also higher (p < 0.10) for HDG than for groups, and were slaughtered at 170 kg of live weight. LDG calves. However, the enzymatic activities, expressed Energy intake level in the feeding period was 2.4 x as per gram or per protein of the pancreas and the small maintenance in 105 days for HDG and 1.4 x main­ intestinal mucosa, were not affected (p > 0.10) by the tenance in 216 days for LDG calves. Total length of the plane of nutrition. These results suggest that the digestive small intestine was identical between groups, but both enzyme activity in the small intestine varies primarily weights of the pancreas and of the small intestinal with the weight of tissues synthesizing the enzyme. mucosa were greater (p < 0.01) for HDG calves. Alpha­ (Key Words: Nutritional Level, Digestive Enzyme, Calf) amylase, lipase, proteinase, and trypsin activities of the INTRODUCTION MATERIALS AND METHODS Ruminant digestion is characterized by microbial Animals and management fermentation in the rumen, the first chamber of the Six Holstein heifer calves weaned at 45 days-of-age stomach and main digestive site. However, digestion by (average live weight, 52 kg) were randomly allocated into host enzymes in the lumen of the small intestine is also a high daily gain group (HDG) or low daily gain group indispensable for nutrient utilization. The enzymes related (LDG), each comprising three calves. HDG calves had to the latter digestion originate in the pancreas and the access to concentrate and Italian ryegrass hay ad libitum. mucosa of the small intestine. And while the influence The same diet at the same ratio (concentrate : hay) was of diet on the activities of these enzymes has been fed to LDG calves, but in a quantity allowing only half widely investigated in monogastric animals, it has only the body-weight gain of HDG calves. LDG calves were rarely been examined in ruminants (Harmon, 1992b). weighed weekly to adjust their feed supply. All calves Kreikemeier et al. (1990) slaughtered steers of different were housed in individual calf hatches with free access to body weights and found that enzymatic activity in their fresh water, and were fed in two equal installments at small intestines was affected by energy consumption level 09:00 and 17:00. The concentrate was purchased com­ via weight changes in the tissues responsible for enzyme mercially, and had a stated proportion of ingredients as synthesis. However, as the tissue weight may vary with follows: 50% grains, 35% protein supplements, and 15% both energy consumption level and body weight, the mineral supplements and other by-products. Crude protein direct influence of energy intake on enzymatic activity is in dry matter was 22.7% in the concentrate and 10.6% in unclear. In this study, therefore, calves were fed a high or hay. The whole mixed diet contained 71% of TDN, in air low energy-level diet and slaughtered at the same body dry matter, which was measured by a direct digestion trial weight prior to examination of the enzymatic activity and immediately before slaughter. The maintenance energy tissue weights of the pancreas and samll intestinal mucosa. requirements of calves were as listed in the Japanese Feeding Standard (Agriculture, Forestry and Fisheries Research Council Secretariat, 1987). 1 Address reprint requests to K. Taniguchi. 2 Graduate Course of International Cooperation, Higashi- hiroshima 739, Japan. Received December 4, 1997; Accepted February 19, 1998 AJAS 1998 Vol. 11 (No. 4) 375-380 376 WANG ET AL. Slaughter and tissue collection by the methods of Kreikemeier et al. (1990) and All calves were slaughtered at approximately 170 kg Bergmeyer et al. (1974). One unit of disaccharidase of live weight by bleeding under general anesthesia with activity was defined as that which hydrolysed one “mol sodium pentobarbital injection after 2 hours of diet disaccharide per min at 37*C. The protein content of the deprivation. Evisceration was performed within appro­ homogenates was assayed by the method of Lowry et al. ximately 20 min after slaughter. The alimentary tracts (1951). were removed and the weights of tracts and remaining A t-test was used to test the difference in enzyme digesta recorded. After the total length of the small activities of the pancreatic and small intestinal mucosa intestine was measured, ten 30-cm segments were taken between each treatment. The effect of the treatment on from the sites at 5, 15, 25, 35, 45, 55, 65, 75, 85, and the distribution pattern of disaccharidase activity along the 95% of the total length. Small intestine and the whole small intestine was analysed by the method of split plot pancreas samples were placed in plastic bags, chilled on analysis using SASD (1990). Inter-treatment dififerences ice, and immediately transported to the laboratory fbr among intestinal site were a nalyzed by t-test. P value further preparation. v 0.10 were considered significant. Sample preparation RESULTS The pancreas was trimmed of excess fat and debris, then weighed and diced. Two grams of pancreatic tissue Mean body weight at slaughter was 172 and 165 kg were combined with 20 ml of cold 0.9% NaCl solution in fbr HDG and LDG, respectively. HDG calves consumed a 50 ml plastic test tube and homogenized by a more concentrate and hay, and showed twice the daily homogenizer (Nihon Seiki Kogyo Co., Tokyo) for 45 s. body-weight gain of LDG calves throughout the feeding The resulting homogenate was centrifuged at 1,300 x g period (table 1). Mean daily intake of TDN was 2.64 kg fbr 10 min. Supernatant of the homogenate was stored at fbr HDG and 1.54 kg fbr LDG calves. LDG calves thus —20*C until determination of a -amylase, lipase, trypsin, required twice as many days to reach the target live chymotrypsin, and proteinase activities. weight. Small intestine were trimmed of excess fat, cut longitudinally, and their mucosa wete rinsed with saline. Table 1. Feed intake and performance of calves After removing excess saline with a piece of filter paper, mucosa were scraped from the small intestine using a Calves Item ------------------------ SEM P glass microscope slide. The scraped mucosa was weighed, HDG1 LDG2 and two grams were combined with 20 ml of cold 0.9% Feed intake3 (kg/d) NaCl solution and homogenized in the same manner used Concentrate 3.45 1.99 0.47 v 0.001 for pancreatic samples. Samples were maintained under Italian ryegrass hay 0.26 0.18 0.03 v 0.004 cold temperature throughout the preparation. Mucosa Total 3.71 2.17 0.50 v 0.001 from each small intestinal site was used to assay fbr Energy level4 2.4 M 1.4 M 0.24 v 0.001 maltase, isomaltase, and lactase activities. Daily gain (kg) 1.09 0.56 0.06 v 0.001 Feeding period (d) 105 216 25 v 0.001 Analyses 1 High Daily Gain. Pancreatic zymogen was activated by enterokinase (E- 2 Low Daily Gain. 5510, Sigma Chemical Co. St. Louis. USA) at 30〔C for 20 3 Mean daily intake. min in 15 mmol/L Tris buffer (pH 8.1). Trypsin and 4 Times of maintenance energy requirement to the mean body chymotrypsin activities were determined photometrically weight for the whole period. using Na-p-toluenesulfbnyl-L-arginine methyl ester (Rick, 1974a) and N-benzoyl-L-tyrosine ethyl ester (Rick, 1974b), The fresh weights of alimentary tracts and digesta are respectively. Proteinase was assayed by the method of shown in table 2. Weights of the tissue of the liver, reticulo- Iwasiro et al. (1992). Alpha-amylase activity in the rumen, omasum-abomasum, and small and laige intestine pancreas was measured by the method of Hall et al. (1970) were greater in HDG calves. Weight of the digesta of the using Starch Azure (S-7776, Sigma Chemical Co.) as small intestine was greater in HDG calves, but that of the substrate. Lipase activity was measured by the method of large intestine was greater in LDG calves. Weights of the Whitaker (1973) using a -naphthyl palmitate as substrate. digesta of the reticulo-rumen and the omasum - abomasum Maltase, isomaltase, and lactase activities were measured were not affected by the nutritional level. DIGESTIVE ENZYME ACTIVITY OF CALVES 377 Table 2. Fresh weights of tissue and digesta of The weight of the pancreas was greater in HDG alimentary tract of calves fed at different nutritional plane calves, but the difference in protein content was not Calves significant (table 3). Enzyme activities, expressed per Item SEM P gram or per protein content, did not differ between HDG HDG1 LDG2 and LDG calves. When enzyme activity was expressed as Tissue weight per body weight (g/kg) total pancreatic activity, however, a -amylase, lipase, Reticulo - rumen 21.5 16.6 0.4 0.041 trypsin, and proteinase activities were greater in HDG Omasum and 9.6 7.8 0.6 0.060 calves. Chymotrypsin also tended to be greater (p < 0.14) abomasum Small intestine 22.3 13.4 2.1 0.002 in HDG calves.
Load more

Recommended publications
  • Disaccharidase Deficiencies
    J Clin Pathol: first published as 10.1136/jcp.s3-5.1.22 on 1 January 1971. Downloaded from J. clin. Path., 24, Suppl. (Roy. Coll. Path.), 5, 22-28 Disaccharidase deficiencies G. NEALE From the Department ofMedicine, Royal Postgraduate Medical School, Du Cane Road, London Up to 12 years ago the absorption of disaccharides capable of hydrolysing maltose, which may explain was a problem in physiology which attracted little why maltase deficiency is not found as an isolated attention and which appeared to be unrelated to the defect of the enterocyte. Isomaltase and sucrase problems of clinical medicine. Indeed, most text- appear to be distinct but linked entities, and hence books stated incorrectly that the disaccharides were they are absent together in the hereditary condition hydrolysed to monosaccharides in the lumen of the of sucrase-isomaltase deficiency (Dahlquist and small intestine despite the evidence of half a century Telenius, 1969). Lactase activity consists of at least before, which had suggested that they were digested two separate enzymes, one of which is not in the by the mucosal surface (Reid, 1901). The renewal of brush border but within the cell (Zoppi, Hadom, interest in the subject of disaccharide absorption Gitzelmann, Kistler, and Prader, 1966). The signifi- occurred after the description of congenital lactase cance of intracellular lactase activity is uncertain. It deficiency by Holzel, Schwarz, and Sutcliffe (1959) cannot play any part in the normal digestion of and of sucrase-isomaltase deficiency by Weijers, lactose which is a function of the brush border of the van de Kamer, Mossel, and Dicke (1960).
    [Show full text]
  • Activation and Detoxification of Cassava Cyanogenic Glucosides by the Whitefly Bemisia Tabaci
    www.nature.com/scientificreports OPEN Activation and detoxifcation of cassava cyanogenic glucosides by the whitefy Bemisia tabaci Michael L. A. E. Easson 1, Osnat Malka 2*, Christian Paetz1, Anna Hojná1, Michael Reichelt1, Beate Stein3, Sharon van Brunschot4,5, Ester Feldmesser6, Lahcen Campbell7, John Colvin4, Stephan Winter3, Shai Morin2, Jonathan Gershenzon1 & Daniel G. Vassão 1* Two-component plant defenses such as cyanogenic glucosides are produced by many plant species, but phloem-feeding herbivores have long been thought not to activate these defenses due to their mode of feeding, which causes only minimal tissue damage. Here, however, we report that cyanogenic glycoside defenses from cassava (Manihot esculenta), a major staple crop in Africa, are activated during feeding by a pest insect, the whitefy Bemisia tabaci, and the resulting hydrogen cyanide is detoxifed by conversion to beta-cyanoalanine. Additionally, B. tabaci was found to utilize two metabolic mechanisms to detoxify cyanogenic glucosides by conversion to non-activatable derivatives. First, the cyanogenic glycoside linamarin was glucosylated 1–4 times in succession in a reaction catalyzed by two B. tabaci glycoside hydrolase family 13 enzymes in vitro utilizing sucrose as a co-substrate. Second, both linamarin and the glucosylated linamarin derivatives were phosphorylated. Both phosphorylation and glucosidation of linamarin render this plant pro-toxin inert to the activating plant enzyme linamarase, and thus these metabolic transformations can be considered pre-emptive detoxifcation strategies to avoid cyanogenesis. Many plants produce two-component chemical defenses as protection against attacks from herbivores and patho- gens. In these plants, protoxins that are ofen chemically protected by a glucose residue are activated by an enzyme such as a glycoside hydrolase yielding an unstable aglycone that is toxic or rearranges to form toxic products1.
    [Show full text]
  • Disaccharidase Deficiency and Malabsorption of Carbohydrates
    SINGAPORE MEDICAL JOURNAL DISACCHARIDASE DEFICIENCY AND MALABSORPTION OF CARBOHYDRATES C K Lee SYNOPSIS A large proportion of man's caloric intake is carbohydrate and starch and sucrose account for over three-quarters of the total consumed. But the rapid change of the food industry from an art to a high specialised industry in recent years have made available a variety of rare food sugars, amongst which are various disacharides. Since the digestion or enzymic breakdown of carbohydrates is a normal initial requirement that precedes their absorption, and metabolism of carbohydrates varies according to their molecular structure, these rare sugars can cause diseases of carbohydrate intolerance and malabsorption. Intolerance and malabsorption can be due to polysaccharide intolerance because of amylase dy- sfunction (caused by the absence of pancreatic amylases) or malfunctioning of absorptive process (caused by damaged or atrophied absorptive mucosa as a result of another primary disease or a variety of other casautive agents or factors, thus resulting in the Department of Chemistry inability of carbohydrate absorption by the alimentary system). A National University of Singapore third type of intolerance is due to primary deficiency or impaired Kent Ridge activity of digestive disaccharidases of the small intestine. The Singapore 0511 physiological significance and the metabolic consequences of such a lactase, sucrase-isomaltase, mal- C K Lee, Ph.D., F.I.F.S.T., C.Chem. F.R.S.C. deficiency or impaired activity of Senior Lecturer tase and trehalase are discussed. 6 VOLUME 25 NO.1 FEBRUARY 19M INTRODUCTION abundance in the free state. It is a constituent of the important plant and animal reserve sugars, starch and Recent years have seen a considerable advance in all glycogen.
    [Show full text]
  • Congenital Sucrase-Isomaltase Deficiency: What, When, and How?
    October 2020 Volume 16, Issue 10, Supplement 5 Congenital Sucrase-Isomaltase Deficiency: What, When, and How? William D. Chey, MD, AGAF, FACG, FACP Professor of Medicine University of Michigan Health System Ann Arbor, Michigan Brooks Cash, MD Dan and Lille Sterling Professor of Gastroenterology Chief, Division of Gastroenterology, Hepatology, and Nutrition University of Texas Health Science Center at Houston Houston, Texas Anthony Lembo, MD Professor of Medicine Harvard Medical School Boston, Massachusetts Daksesh B. Patel, DO Illinois Gastroenterology Group/GI Alliance Chief, Division of Gastroenterology and Hepatology AMITA St Francis Hospital Evanston, Illinois Accredited by Rehoboth McKinley Christian Health Care Services Kate Scarlata, RDN, LDN Owner, For a Digestive Peace of Mind, LLC Digestive Health Nutrition Consulting Medway, Massachusetts A CME Activity Approved for 1.0 AMA PRA Category 1 CreditTM Provided by the Gi Health Foundation Release Date: October 2020 ON THE WEB: Expiration Date: gastroenterologyandhepatology.net October 31, 2021 Supported by an Estimated time to educational grant from Indexed through the National Library of Medicine complete activity: QOL Medical, LLC (PubMed/Medline), PubMed Central (PMC), and EMBASE 1.0 hour Congenital Sucrase-Isomaltase Deficiency: What, When, and How? To claim 1.0 AMA PRA Category 1 CreditTM for this activity, please visit: gihealthfoundation.org/CSIDMONOGRAPH Target Audience Disclosures This CME monograph will target gastroenterologists, primary care physi- Faculty members are required to inform the audience when they are dis- cians, nurse practitioners, physician assistants, and nurses. cussing off-label, unapproved uses of devices and drugs. Physicians should consult full prescribing information before using any product mentioned Goal Statement during this educational activity.
    [Show full text]
  • Protein-Carbohydrate Interactions Leading to Hydrolysis and Transglycosylation in Plant Glycoside Hydrolase Family 1 Enzymes
    J. Appl. Glycosci., 59, 51‒62 (2012) doi: 10.5458/jag.jag.JAG-2011_022 ©2012 The Japanese Society of Applied Glycoscience Review Protein-carbohydrate Interactions Leading to Hydrolysis and Transglycosylation in Plant Glycoside Hydrolase Family 1 Enzymes (Received December 7, 2011; Accepted January 30, 2012) (J-STAGE Advance Published Date: February 11, 2012) James R. Ketudat Cairns,1,＊ Salila Pengthaisong,1 Sukanya Luang,1 Sompong Sansenya, 1 Anupong Tankrathok1 and Jisnuson Svasti2 1Schools of Biochemistry and Chemistry, Institute of Science, Suranaree University of Technology (Muang District, Nakhon Ratchasima 30000, Thailand) 2Department of Biochemistry and Centre for Protein Structure and Engineering, Faculty of Science, Mahidol University (Phayathai, Bangkok 10400, Thailand) Abstract: Glycoside hydrolase family 1 (GH1) includes enzymes with a wide range of specifi cities in terms of reactions, substrates and products, with plant GH1 enzymes covering a particularly wide range of hy- drolases and transglycosylases. In plants, in addition to β-D-glucosidases, β-D-mannosidases, disacchari- dases, thioglucosidases and hydroxyisourate hydrolase, GH1 has recently been found to include galactosyl and glucosyl transferases that utilize galactolipid and acyl glucose donors, respectively. The amino acids binding to the nonreducing monosaccharide residue of glycosides and oligosaccharides in subsite －1 are largely conserved in GH1 glycoside hydrolases, despite their different glycon specifi cities, and residues outside this subsite contribute to sugar specifi city. The conserved subsite －1 residues form extensive hy- drogen bonding and aromatic stacking interactions to the glycon to distort it toward the transition state, so they must make different interactions with different sugars. Aglycon specifi city is largely determined by interactions with the cleft leading into the active site, but different enzymes appear to interact with their substrates via different residues.
    [Show full text]
  • Inhibition of Activities of Individual Subunits of Intestinal Maltase-Glucoamylase and Sucrase-Isomaltase by Dietary Phenolic
    Purdue University Purdue e-Pubs Open Access Dissertations Theses and Dissertations January 2014 INHIBITION OF ACTIVITIES OF INDIVIDUAL SUBUNITS OF INTESTINAL MALTASE-GLUCOAMYLASE AND SUCRASE-ISOMALTASE BY DIETARY PHENOLIC COMPOUNDS FOR MODULATING GLUCOSE RELEASE AND GENE RESPONSE Meric Simsek Purdue University Follow this and additional works at: https://docs.lib.purdue.edu/open_access_dissertations Recommended Citation Simsek, Meric, "INHIBITION OF ACTIVITIES OF INDIVIDUAL SUBUNITS OF INTESTINAL MALTASE-GLUCOAMYLASE AND SUCRASE-ISOMALTASE BY DIETARY PHENOLIC COMPOUNDS FOR MODULATING GLUCOSE RELEASE AND GENE RESPONSE" (2014). Open Access Dissertations. 1500. https://docs.lib.purdue.edu/open_access_dissertations/1500 This document has been made available through Purdue e-Pubs, a service of the Purdue University Libraries. Please contact [email protected] for additional information. Graduate School Form 30 (Updated 11/20/2014) PURDUE UNIVERSITY GRADUATE SCHOOL Thesis/Dissertation Acceptance This is to certify that the thesis/dissertation prepared By Meric Simsek Entitled INHIBITION OF ACTIVITIES OF INDIVIDUAL SUBUNITS OF INTESTINAL MALTASE-GLUCOAMYLASE AND SUCRASE-ISOMALTASE BY DIETARY PHENOLIC COMPOUNDS FOR MODULATING GLUCOSE RELEASE AND GENE RESPONSE Doctor of Philosophy For the degree of Is approved by the final examining committee: Bruce R. Hamaker Mario G. Ferruzzi Kee-Hong Kim Roberto Quezada-Calvillo To the best of my knowledge and as understood by the student in the Thesis/Dissertation Agreement, Publication Delay, and Certification/Disclaimer (Graduate School Form 32), this thesis/dissertation adheres to the provisions of Purdue University’s “Policy on Integrity in Research” and the use of copyrighted material. Bruce R. Hamaker Approved by Major Professor(s): ____________________________________ ____________________________________ 11/21/2014 Approved by: Mario G.
    [Show full text]
  • Coffea Arabica Bean Extract Inhibits Glucose Transport and Disaccharidase Activity in Caco‑2 Cells
    BIOMEDICAL REPORTS 15: 73, 2021 Coffea arabica bean extract inhibits glucose transport and disaccharidase activity in Caco‑2 cells ATCHARAPORN ONTAWONG1, ACHARAPORN DUANGJAI1 and CHUTIMA SRIMAROENG2 1Division of Physiology, School of Medical Sciences, University of Phayao, Muang Phayao, Phayao 56000; 2Department of Physiology, Faculty of Medicine, Chiang Mai University, Chiang Mai, Nong Khai 52000, Thailand Received February 3, 2021; Accepted June 14, 2021 DOI: 10.3892/br.2021.1449 Abstract. The major constituents of Coffea arabica (coffee), or sucrase‑isomaltase cleaves the α‑glucoside bonds of including caffeine, chlorogenic acid and caffeic acid, exhibit disaccharides, including sucrose, to monosaccharides. The antihyperglycemic properties in in vitro and in vivo models. absorption of dietary monosaccharides by the intestine may However, whether Coffea arabica bean extract (CBE) regu‑ be one of the risk factors associated with diabetes mellitus (1). lates glucose uptake activity and the underlying mechanisms Glucose derived from starch or sucrose is taken up by the involved remain unclear. The aim of the present study was epithelial cells through the brush border membrane (BBM), to examine the effects of CBE on glucose absorption and predominantly by a sodium‑dependent glucose co‑transporter identify the mechanisms involved using an in vitro model. (SGLT1) (2,3). A previous study has revealed that glucose The uptake of a fluorescent glucose analog into Caco‑2 transporter 2 (GLUT2) is expressed at the BBM of enterocytes colorectal adenocarcinoma cells was determined. The expres‑ during the digestive phase and may affect circulatory glucose sion levels of sodium glucose co‑transporter 1 (SGLT1) and concentration (2). Subsequently, glucose effluxes across the baso‑ glucose transporter 2 (GLUT2) were evaluated.
    [Show full text]
  • This Thesis Has Been Submitted in Fulfilment of the Requirements for a Postgraduate Degree (E.G
    This thesis has been submitted in fulfilment of the requirements for a postgraduate degree (e.g. PhD, MPhil, DClinPsychol) at the University of Edinburgh. Please note the following terms and conditions of use: This work is protected by copyright and other intellectual property rights, which are retained by the thesis author, unless otherwise stated. A copy can be downloaded for personal non-commercial research or study, without prior permission or charge. This thesis cannot be reproduced or quoted extensively from without first obtaining permission in writing from the author. The content must not be changed in any way or sold commercially in any format or medium without the formal permission of the author. When referring to this work, full bibliographic details including the author, title, awarding institution and date of the thesis must be given. Interaction of Bacteroides fragilis with Host Proteins and Effects of Nitrogen Limitation on the B. fragilis Transcriptome Aparna Shankar Thesis presented for the degree of Doctor of Philosophy Institute of Cell Biology The University of Edinburgh November 2015 Declaration The author performed all of the investigations and procedures presented in this thesis, unless otherwise stated. APARNA SHANKAR i Acknowledgements I would like to take this opportunity to express my sincere gratitude to each and everyone who made this four year journey worthwhile and unforgettable. To begin with, I thank my supervisor Dr. Garry Blakely for giving me an opportunity to pursue doctoral research in his lab. It was definitely his constant encouragement, valuable suggestions and enthusiasm for science that kept me going. I would also like to thank my second supervisor, Dr.
    [Show full text]
  • Influence of Exocrine and Endocrine Pancreatic Function on Intestinal Brush Border Enzymatic Activities1
    Gut: first published as 10.1136/gut.16.2.89 on 1 February 1975. Downloaded from Gut, 1975, 16, 89-92 Influence of exocrine and endocrine pancreatic function on intestinal brush border enzymatic activities1 W. F. CASPARY, K. WINCKLER, P. G. LANKISCH, AND W. CREUTZFELDT From the Division of Gastroenterology and Metabolism, Department of Medicine, University of Gdttingen, Germany SUMMARY Digestive enzymatic activities (disaccharidases, alkaline phosphatase, peptide hydrolases) have been determined in the mucosa of 14 patients with chronic pancreatitis. All had an abnormal secretin-pancreozymin test. Four patients had insulin-dependent diabetes mellitus, four a patho- logical glucose tolerance test. Nine patients had steatorrhoea. Maltase, sucrase, and alkaline phos- phatase activity was significantly elevated in patients with exocrine pancreatic insufficiency, whereas those of lactase, trehalase, and peptide hydrolase were normal. Patients with steatorrhoea had higher maltase and sucrase activity than those without steatorrhoea, whereas decreased glucose tolerance had no effect on brush border enzymatic activity. It is suggested that decreased exocrine rather than decreased endocrine pancreatic function is responsible for the increase in intestinal disaccharidase and alkaline phosphatase activity, possibly by the influence of pancreatic enzymes on the turnover of brush border enzymes from the luminal side of the mucosal membrane or by direct hormonal stimulation through cholecystokinin. http://gut.bmj.com/ An increased digestive and absorptive function has estimated in small bowel biopsies from patients been found in the small intestine of rats with experi- with chronic pancreatitis and an abnormal secretin- mentally induced alloxan (Crane, 1961; Hossain, pancreozymin test with and without diabetes Levinson, and Englert, 1970; Olson and Rogers, mellitus.
    [Show full text]
  • The Enzyme Database: New Enzymes 06/27/2006 05:11 PM
    The Enzyme Database: New Enzymes 06/27/2006 05:11 PM Home Search Enzymes by Class New/Amended Enzymes Statistics Forms Advanced Search Information Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) Proposed Changes to the Enzyme List The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC- IUBMB by Keith Tipton, Sinéad Boyce, Gerry Moss and Hal Dixon, with occasional help from other Committee members, and were put on the web by Gerry Moss. Comments and suggestions on these draft entries should be sent to Professor K.F. Tipton and Dr S. Boyce (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland) by 20 May 2006, after which, the entries will be made official and will be incorporated into the main enzyme list. To prevent confusion please do not quote new EC numbers until they are incorporated into the main list. Many thanks to those of you who have submitted details of new enzymes or updates to existing enzymes. An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry. Contents *EC 1.1.1.262 4-hydroxythreonine-4-phosphate dehydrogenase EC 1.1.1.289 sorbose reductase EC 1.1.1.290 4-phosphoerythronate dehydogenase EC 1.1.99.19 transferred *EC 1.2.1.10 acetaldehyde dehydrogenase (acetylating) EC 1.2.1.71 succinylglutamate-semialdehyde dehydrogenase EC 1.2.1.72 erythrose-4-phosphate dehydrogenase EC 1.2.99.1 transferred *EC 1.3.99.19 quinoline-4-carboxylate 2-oxidoreductase
    [Show full text]
  • Wjcc.V9.I17.4178 ISSN 2307-8960 (Online)
    World Journal of W J C C Clinical Cases Submit a Manuscript: https://www.f6publishing.com World J Clin Cases 2021 June 16; 9(17): 4178-4187 DOI: 10.12998/wjcc.v9.i17.4178 ISSN 2307-8960 (online) ORIGINAL ARTICLE Observational Study Patients with functional bowel disorder have disaccharidase deficiency: A single-center study from Russia Saria Dbar, Olga Akhmadullina, Elena Sabelnikova, Nikolai Belostotskiy, Asfold Parfenov, Svetlana Bykova, Sergey Bakharev, Elena Baulo, Alexandra Babanova, Lilia Indeykina, Tatyana Kuzmina, Tatiana Kosacheva, Aleksey Spasenov, Alina Makarova ORCID number: Saria Dbar 0000- Saria Dbar, Olga Akhmadullina, Svetlana Bykova, Sergey Bakharev, Elena Baulo, Alexandra 0001-6516-7782; Olga Akhmadullina Babanova, Tatiana Kosacheva, Non-inflammatory Bowel Diseases, Moscow Health Department, 0000-0002-4010-6761; Elena Moscow Clinical Scientific Center n.a. A.S. Loginov, Moscow 111123, Russia Sabelnikova 0000-0001-7519-2041; Nikolai Belostotskiy 0000-0003-4400- Elena Sabelnikova, Moscow Health Department, Moscow Clinical Scientific Center n.a. A.S. 1227; Asfold Parfenov 0000-0002- Loginov, Moscow 111123, Russia 9782-4860; Svetlana Bykova 0000- 0001-9576-2953; Sergey Bakharev Nikolai Belostotskiy, Pre-Clinical Research Laboratory, Moscow Clinical Scientific Center 0000-0003-2213-6147; Elena Baulo Named after A.S. Loginov MHD, Moscow 111123, Russia 0000-0002-8300-7608; Alexandra Babanova 0000-0001-9263-8324; Lilia Asfold Parfenov, Department of Bowel Pathology, Moscow Health Department, Moscow Indeykina 0000-0002-3829-3211; Clinical Scientific Center n.a. A.S. Loginov, Moscow 111123, Russia Tatyana Kuzmina 0000-0003-2800- 6503; Tatiana Kosacheva 0000-0002- Lilia Indeykina, Alina Makarova, Laboratory of Functional Diagnostics of Intestinal Diseases, 4951-0605; Aleksey Spasenov 0000- Moscow Health Department, Moscow Clinical Scientific Center n.a.
    [Show full text]
  • Intestinal Β-Galactosidases: II. Biochemical Alteration in Human Lactase Deficiency
    Intestinal β-galactosidases: II. Biochemical alteration in human lactase deficiency Gary M. Gray, … , Eugene H. Colver, Myron Genel J Clin Invest. 1969;48(4):729-735. https://doi.org/10.1172/JCI106030. Despite the high prevalence of intestinal lactase deficiency in some racial groups and in patients with intestinal disease, the biochemical defect has not been characterized. In the preceding paper normal intestine was found to have two lactases with distinctly different pH optima. Therefore, pH activity curves of homogenates from lactase-deficient intestine were studied, and the pH optimum was found to be shifted from the normal of 5.8 to 4.8. Density gradient ultracentrifugation of intestinal material from five lactase-deficient patients demonstrated absence of a lactase with pH optimum 6.0 and molecular weight 280,000. A second lactase with pH optimum 4.5 and molecular weights of 156,000 and 660,000 remained at normal levels accounting for the shift in the pH optimum in whole intestinal homogenates. In addition, three of the five patients had absence of a smaller β-galactosidase (molecular weight 80,000) that had specificity only for synthetic substrates. Although not a lactase, this enzyme had a pH optimum identical with the missing lactase, and its activity was inhibited by lactose in a partially competitive manner suggesting that it is capable of binding lactose. It is possible that this enzyme is a precursor or fragment of the missing lactase. The residual lactase activity provided by the lactase with low pH optimum represents 20-70% of the activity of the missing enzyme, and yet these patients […] Find the latest version: https://jci.me/106030/pdf Intestinal /3-Galactosidases II.
    [Show full text]