DOCSLIB.ORG

Congenital Sucrase-Isomaltase Deficiency (CSID)

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Congenital Sucrase-Isomaltase Deficiency (CSID) ANMC Congenital Sucrase-Isomaltase Deficiency (CSID) Diagnosis and Treatment Guidelines Updated 8/19/20 Background Information1 Symptoms1 Diagnosis¹ 2 • It is estimated that 3-10% of Alaska Native people • Osmotic diarrhea • Malnutrition • Genetic screen (blood) through have CSID, but exact prevalence is unknown • Abdominal pain & distention • Failure to thrive Fulgent Genetics • There is a mutation present in people from Arctic • Click here for test requisition and regions that results in a complete lack of enzyme Symptoms vary between affected individuals depending on here for consent form activity the amount of sucrose and/or starch consumed and other • In the Test Requested box write • Higher prevalence of CSID is seen along the unknown factors “SI gene c.273_274delAG western/northern coasts of the state, especially Other Considerations p.Gly92Leufs*8” Yup’ik and Inupiaq people Can onset of symptoms be traced back to introduction of • Cost: $200 • CSID is an autosomal recessive (homozygous) table foods? Breast and most formula fed infants are • 2-3 week turnaround for results disorder, but heterozygote carriers may also be asymptomatic • symptomatic Is there a family history of intolerance or “allergy” to Consider full sequencing of SI gene if • ANTHC has a CSID Program to provide education sugar? known mutation test is negative and and support for patients, families, and providers* Are symptoms worse when eating store bought foods symptoms still indicate possible CSID • • Click here to access the Pocket Guide to Alaska versus Alaska Native traditional foods? Notify CSID Program Coordinator with Native Pediatric Diagnoses positive results Nutrition Infant Formulas Medication Management3 Prescribing Sucraid® • Avoid and/or limit sucrose (table sugar) and • Breast milk and standard • Sacrosidase (Sucraid®): enzyme replacement • If prescribing for starch lactose based formulas, for sucrase patients located in the • The Alaska Native traditional diet is excellent such as Similac® • Taken with each meal and snack that Anchorage Service Unit for managing symptoms of CSID since it is Advance® or Enfamil® contain sucrose click here for naturally low in sucrose and starch Infant, are typically • Dosage is weight dependent instructions • Refer patient to a Registered Dietitian tolerated • Requires refrigeration • If prescribing for • If no RD available, refer to CSID • Most other formulas • Most private insurance covers patients in the Program Coordinator contain sucrose and/or Sucraid® Utqiagvik, Kotzebue, • CSID education materials for starch and are generally • For Medicaid or IHS recipients, refer and Nome Service Unit patients/families are available. Contact the not tolerated patient to ANTHC’s Tribally Sponsored check for Sucraid® CSID Program Coordinator for copies. Health Insurance Program (TSHIP). See availability with the TSHIP section local pharmacy *For questions or assistance, contact ANTHC’s CSID Outreach and Education Coordinator at 729-3628 Tribally Sponsored Health Insurance Program (TSHIP) REFERENCES: 1. Marcadier, J., Boland, M., Scott, C., Issa, K., Wu, Z., McIntyre, A., Hegele, R., Geraghty, • ANTHC partners with THOs to sponsor eligible individuals for health M. and Lines, M. (2014). Congenital sucrase–isomaltase deficiency: identification of a common Inuit insurance coverage founder mutation. Canadian Medical Association Journal, 187(2), pp.102-107. 2. Treem, W. (2012). Clinical Aspects and Treatment of Congenital Sucrase-Isomaltase Deficiency. Journal of Pediatric • Covers the cost of Sucraid® Gastroenterology and Nutrition, 55, pp.S7-S13. 3. Sucraid for Healthcare Providers. (2018). Sucraid® - • 2-6 week period between enrollment and effective coverage Information for Healthcare Providers. [online] Available at: https://www.sucraid.net/hcp/ [Accessed • Does not provide retroactive coverage 10 Sep. 2018]. • Refer patient to TSHIP by calling 729-2935. A Health Benefits Specialist will work with the patient for eligibility verification and enrollment.
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]
  • SI Gene Sucrase-Isomaltase
    SI gene sucrase-isomaltase Normal Function The SI gene provides instructions for producing the enzyme sucrase-isomaltase. This enzyme is found in the intestinal tract, where it is involved in breaking down the sugars sucrose (a sugar found in fruits, and also known as table sugar) and maltose (the sugar found in grains). Sucrose and maltose are called disaccharides because they are each made up of two simple sugar molecules. Disaccharides must be broken down into simple sugar molecules to be digested properly. The sucrase-isomaltase enzyme is found on the surface of the intestinal epithelial cells, which are cells that line the walls of the intestine. These cells have fingerlike projections called microvilli that absorb nutrients from food as it passes through the intestine. Based on their appearance, groups of these microvilli are known collectively as the brush border. The role of the sucrase-isomaltase enzyme is to break down sucrose and maltose into simple sugars so that they can be absorbed by microvilli into intestinal epithelial cells. Health Conditions Related to Genetic Changes Congenital sucrase-isomaltase deficiency At least 10 mutations in the SI gene have been found to cause congenital sucrase- isomaltase deficiency. These mutations disrupt the folding and processing of the sucrose-isomaltase enzyme, transportation of the enzyme within the intestinal epithelial cells, the orientation of the enzyme to the cell surface, or its normal functioning. An impairment in any of these cell processes results in a sucrase-isomaltase enzyme that cannot effectively break down sucrose, maltose, or other compounds made from these sugar molecules (carbohydrates).
    [Show full text]
  • Is There Hidden Sugar in Your Drink?
    Is There Hidden Sugar in Your Drink? Anjali Shankar 9th Grade Moravian Academy Upper School June 5th, 2020 Motivation - I have a big passion for the medical field, showed by last year’s project. - Food labels and nutrition have caught my eye and are important when eating. How do glucose levels Research in different drinks change after adding Question an invertase enzyme? Given that the invertase enzyme breaks down sucrose, glucose levels will rise after adding the enzyme because the sucrose will convert to Hypothesis glucose and fructose. Coca Cola will have the most glucose because it has the most calories of each drink. Glucose - Chemical compound in the body - C6H12O6 - Comes from food and drink - Generally rich in sugars/carbohydrates - Used for many purposes: - Used to make energy (ATP) in cellular respiration - Stores energy - Used to build carbohydrates Chemical Reaction - A chemical reaction transfers a set of compounds into another - Reactants: Enter into a chemical reaction - Products: Compounds produced by the reaction - Catalyst: Speeds up the rate of a chemical reaction - Enzyme: Biological catalysts; usually proteins The formula for this experiment is: Invertase Sucrose + Water Glucose + Fructose Invertase C12H22O11 + H20 C6H12O6 + C6H12O6 In the Body - The most common sugar is eaten as sucrose. - Also known as table sugar - It is broken down in the body into glucose and fructose through a chemical reaction during digestion. - Fructose: Contains the same elements as glucose, but has a different chemical construction - Often used to make more glucose - The reaction is catalyzed by an enzyme named sucrase. - Modeled by invertase in experiment - The pancreas monitors blood sugar, or amount of glucose in the body.
    [Show full text]
  • Ep 2 246 408 A2
    (19) & (11) EP 2 246 408 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 03.11.2010 Bulletin 2010/44 C09K 8/60 (2006.01) (21) Application number: 10158819.2 (22) Date of filing: 13.11.2000 (84) Designated Contracting States: • Norman, Monica AT BE CH CY DE DK ES FI FR GB GR IE IT LI LU Houston, TX 77041 (US) MC NL PT • Symes, Kenneth C. Designated Extension States: Bradford, RO Yorkshire BD14 6LR (GB) • Mistry, Kishor K. (30) Priority: 12.11.1999 US 165393 P Keighley, East Moton, BD20 5UU (GB) (62) Document number(s) of the earlier application(s) in • Ballard, David A. accordance with Art. 76 EPC: Stonehaven, 00980356.0 / 1 232 329 Aberdeenshire AB39 3PQ (GB) (27) Previously filed application: (74) Representative: Hull, John Philip 13.11.2000 PCT/US03/01106 Beck Greener Fulwood House (71) Applicant: M-I L.L.C. 12 Fulwood Place Houston, TX 77072 (US) London WC1V 6HR (GB) (72) Inventors: Remarks: • Freeman, Michael A. This application was filed on 31-03-2010 as a Kingwood, TX 77345 (US) divisional application to the application mentioned • Jiang, Ping under INID code 62. 3400 Sandnes (NO) (54) Method and composition f or the triggered release of polymer-degrading agents for oil field use (57) Disclosed are methods and related composi- tions for altering the physical and chemical properties of a substrate used in hydrocarbon exploitation, such as in downhole drilling operations. In a preferred embodiment a method involves formulating a fluid, tailored to the spe- cific drilling conditions, that contains one or more inacti- vated enzymes.
    [Show full text]
  • Congenital Sucrase-Isomaltase Deficiency
    Congenital sucrase-isomaltase deficiency Description Congenital sucrase-isomaltase deficiency is a disorder that affects a person's ability to digest certain sugars. People with this condition cannot break down the sugars sucrose and maltose. Sucrose (a sugar found in fruits, and also known as table sugar) and maltose (the sugar found in grains) are called disaccharides because they are made of two simple sugars. Disaccharides are broken down into simple sugars during digestion. Sucrose is broken down into glucose and another simple sugar called fructose, and maltose is broken down into two glucose molecules. People with congenital sucrase- isomaltase deficiency cannot break down the sugars sucrose and maltose, and other compounds made from these sugar molecules (carbohydrates). Congenital sucrase-isomaltase deficiency usually becomes apparent after an infant is weaned and starts to consume fruits, juices, and grains. After ingestion of sucrose or maltose, an affected child will typically experience stomach cramps, bloating, excess gas production, and diarrhea. These digestive problems can lead to failure to gain weight and grow at the expected rate (failure to thrive) and malnutrition. Most affected children are better able to tolerate sucrose and maltose as they get older. Frequency The prevalence of congenital sucrase-isomaltase deficiency is estimated to be 1 in 5, 000 people of European descent. This condition is much more prevalent in the native populations of Greenland, Alaska, and Canada, where as many as 1 in 20 people may be affected. Causes Mutations in the SI gene cause congenital sucrase-isomaltase deficiency. The SI gene provides instructions for producing the enzyme sucrase-isomaltase.
    [Show full text]
  • Characterization of Substrate Binding and Catalytic Mechanisms of An
    Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 1988 Characterization of substrate binding and catalytic mechanisms of an endoxylanase, amylosucrase, and porcine pancreatic alpha-amylase Bernard Yi Tao Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biochemistry Commons, and the Chemical Engineering Commons Recommended Citation Tao, Bernard Yi, "Characterization of substrate binding and catalytic mechanisms of an endoxylanase, amylosucrase, and porcine pancreatic alpha-amylase " (1988). Retrospective Theses and Dissertations. 8807. https://lib.dr.iastate.edu/rtd/8807 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. INFORMATION TO USERS The most advanced technology has been used to photo­ graph and reproduce this manuscript from the microfilm master, UMI films the original text directly fi'om the copy submitted. Thus, some dissertation copies are in typewriter face, while others may be from a computer printer. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyrighted material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are re­ produced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overlaps.
    [Show full text]
  • Digestion of Carbohydrates
    Digestion of carbohydrates Alongside fat and protein, carbohydrates are one of the three macronutrients in our diet with their main function being to provide energy to the body. They occur in many different forms, like sugars and dietary fibre, and in many different foods, such as whole grains, fruit and vegetables. Digesting or metabolizing carbohydrates breaks foods down into sugars, which are also called saccharides. These molecules begin digesting in the mouth and continue through the body to be used for anything from normal cell functioning to cell growth and repair. It is also directly used as energy source in muscle, brain and other cells. Dietary carbohydrate principally consists of …. Polysaccharides: - Starch, glycogen and cellulose Disaccharides: - Sucrose and maltose Monosaccharide:-Glucose and fructose Out of these three types of carbohydrates, monosaccharide does not need digestion. Digestion of carbohydrates During digestion, carbohydrates that consist of more than one sugar get broken down into their monosaccharides by digestive enzymes, and then get directly absorbed causing a glycaemic response. Some of the carbohydrates cannot be broken down and they get either fermented by our gut bacteria or they transit through the gut without being changed. Digestive enzymes and their source Mouth: - Salivary amylase (α-amylase, Ptyalin) Stomach: - No enzymes Pancreas: - Pancreatic α-amylase Intestine: - Dextrinase, Maltase, Isomaltase, Sucrase, Lactase Digestion in mouth Digestion of carbohydrates starts at the mouth. In mouth,
    [Show full text]
  • Production of Carbohydrases for Developing Soy Meal As
    PRODUCTION OF CARBOHYDRASES FOR DEVELOPING SOY MEAL AS PROTEIN SOURCE FOR ANIMAL FEED A Dissertation Presented to The Graduate Faculty of The University of Akron In Partial Fulfillment Of the Requirements for the Degree Doctor of Philosophy Qian Li May, 2017 PRODUCTION OF CARBOHYDRASES FOR DEVELOPING SOY MEAL AS PROTEIN SOURCE FOR ANIMAL FEED Qian Li Dissertation Approved: Accepted: Advisor Department Chair Dr. Lu-Kwang Ju Dr. Michael H. Cheung Committee Member Dean of the College Dr. Jie Zheng Dr. Donald P. Visco Jr. Committee Member Dean of the Graduate School Dr. Lingyun Liu Dr. Chand Midha Committee Member Date Dr. Ge Zhang Committee Member Dr. Pei-Yang Liu ii ABSTRACT Global demand for seafood is growing rapidly and more than 40% of the demand is met by aquaculture. Conventional aquaculture diet used fishmeal as the protein source. The limited production of fishmeal cannot meet the increase of aquaculture production. Therefore, it is desirable to partially or totally replace fishmeal with less-expensive protein sources, such as poultry by-product meal, feather meal blood meal, or meat and bone meal. However, these feeds are deficient in one or more of the essential amino acids, especially lysine, isoleucine and methionine. And, animal protein sources are increasingly less acceptable due to health concerns. One option is to utilize a sustainable, economic and safe plant protein sources, such as soybean. The soybean industry has been very prominent in many countries in the last 20 years. The worldwide soybean production has increased 106% since 1996 to 2010[1]. Soybean protein is becoming the best choice of sustainable, economic and safe protein sources.
    [Show full text]
  • Structures and Characteristics of Carbohydrates in Diets Fed to Pigs: a Review Diego M
    Navarro et al. Journal of Animal Science and Biotechnology (2019) 10:39 https://doi.org/10.1186/s40104-019-0345-6 REVIEW Open Access Structures and characteristics of carbohydrates in diets fed to pigs: a review Diego M. D. L. Navarro1, Jerubella J. Abelilla1 and Hans H. Stein1,2* Abstract The current paper reviews the content and variation of fiber fractions in feed ingredients commonly used in swine diets. Carbohydrates serve as the main source of energy in diets fed to pigs. Carbohydrates may be classified according to their degree of polymerization: monosaccharides, disaccharides, oligosaccharides, and polysaccharides. Digestible carbohydrates include sugars, digestible starch, and glycogen that may be digested by enzymes secreted in the gastrointestinal tract of the pig. Non-digestible carbohydrates, also known as fiber, may be fermented by microbial populations along the gastrointestinal tract to synthesize short-chain fatty acids that may be absorbed and metabolized by the pig. These non-digestible carbohydrates include two disaccharides, oligosaccharides, resistant starch, and non-starch polysaccharides. The concentration and structure of non-digestible carbohydrates in diets fed to pigs depend on the type of feed ingredients that are included in the mixed diet. Cellulose, arabinoxylans, and mixed linked β-(1,3) (1,4)-D-glucans are the main cell wall polysaccharides in cereal grains, but vary in proportion and structure depending on the grain and tissue within the grain. Cell walls of oilseeds, oilseed meals, and pulse crops contain cellulose, pectic polysaccharides, lignin, and xyloglucans. Pulse crops and legumes also contain significant quantities of galacto-oligosaccharides including raffinose, stachyose, and verbascose.
    [Show full text]
  • Purification, Characterization and Gene Analysis of a New Α-Glucosidase from Shiraia Sp
    Ann Microbiol (2017) 67:65–77 DOI 10.1007/s13213-016-1238-y ORIGINAL ARTICLE Purification, characterization and gene analysis of a new α-glucosidase from shiraia sp. SUPER-H168 Ruijie Gao1 & Huaxiang Deng1 & Zhengbing Guan1 & Xiangru Liao1 & Yujie Cai 1 Received: 21 October 2015 /Accepted: 19 October 2016 /Published online: 27 October 2016 # Springer-Verlag Berlin Heidelberg and the University of Milan 2016 Abstract A new α-glucosidase from Shiraia sp. SUPER- Keywords α-glucosidase . Characterization . Gene analysis . H168 under solid-state fermentation was purified by alcohol Purification . Shiraia sp. SUPER-H168 . Solid-state precipitation and anion-exchange and by gel filtration chro- fermentation matography. The optimum pH and temperature of the purified α-glucosidase were 4.5 and 60 °C, respectively, using p- nitrophenyl-α-glucopyranoside (α-pNPG) as a substrate. Introduction Ten millimoles of sodium dodecyl sulfate, Fe2+,Cu2+, and Ag+ reduced the enzyme activity to 0.7, 7.6, 26.0, and Glycoside hydrolases (EC 3.2.1.-) are a widespread group of 6.2 %, respectively, of that of the untreated enzyme. The enzymes that hydrolyze the glycosidic bond between two or Km, Vmax,andkcat/Km of the α-glucosidase were 0.52 mM, more carbohydrates or between a carbohydrate and a non- −1 4 −1 −1 3.76 U mg , and 1.3 × 10 Ls mol ,respectively.Km with carbohydrate moiety. α-glucosidases (EC 3.2.1.20, α-D- maltose was 0.62 mM. Transglycosylation activities were ob- glucoside glucohydrolase) constitute a group of exo-acting served with maltose and sucrose as substrates, while there was glycoside hydrolases of diverse specificities that catalyze the no transglycosylation with trehalose.
    [Show full text]
  • Sucraid Review
    TAB B United States CONSUMER PRODUCT SAFETY COMMISSION Washington, D.C. 20207 APR I 1998 MEMORAh?)UM TO: Mary Ann Danello, Ph.D., Associate Executive Director, Directorate for Epidemiology and Health Sciences THROUGH: Marilyn L. Wind, Ph.D., Director, Division of Health Sciences,w&; Directorate for Epidemiology and Health Sciences FROM: Jacqueline N. Ferrante, Ph.D., Pharmacologist, Division of Health Sciences, JF Directorate for Epidemiology and Health Sciences SUBJECT: Sucraid Review 1 Introduction Orphan Medical petitioned the Commission to exempt SucraidrM, an oral solution of the enzyme sacrosidase, from special packaging requirements for oral prescription drugs under the Poison Prevention Packaging Act (PPPA). This memorandum reviews scientific information related to Sucraidr”. Product Description and Use SucraidTM is the brand name for sacrosidase, a yeast-derived form of the sucrase enzyme. This enzyme is obtained from baker’s yeast which is also known as Saccharomyces cerevisiae. SucraidTM contains 1.5 milligrams (8,500 International Units) per milliliter (mg/ml) of the enzyme in a 5050 solution of glycerol and water at an unbuffered slightly acidic pH of 4.6. SucraidTM is the only available treatment for congenital sucrase-isomaltase deficiency (CSID). It is replacement therapy for sucrase, not isomaltase. The petitioner argues that the confectionery and baking industry has used this enzyme extensively and that under 21 CFR 170.30 it is a “Generally Recognized as Safe” (GRAS) food material because of its long history of safe use in humans. It is used as a flavoring agent and adjuvant at a level not to exceed five percent in food. The recommended dose of SucraidTM for patients with CSID is one ml per meal or snack for patients weighing up to 15 kilograms (kg) (33 pounds) and 2 ml for patients over 15 kg.
    [Show full text]
  • CSID) Symptoms, Diagnosis, and Treatment
    CONGENITAL SUCRASE-ISOMALTASE DEFICIENCY (CSID) Symptoms, Diagnosis, and Treatment FOR ADULT GASTROENTEROLOGISTS PMS 294 2020 QOL Medical, LLC 1 Financial Disclosures o [Disclose financial relationships with manufacturers and medical organizations here (e.g., QOL Medical, LLC); if none, list “None.”] PMS 294 2020 QOL Medical, LLC 2 WHAT IS CSID? PMS 294 2020 QOL Medical, LLC 3 CSID: Congenital Sucrase-Isomaltase Deficiency Sucrase-Isomaltase o An enzyme that digests the majority of dietary carbohydrates o Table sugar (sucrose) and many starches (e.g., potatoes, bread) o Expressed in the microvilli of the brush border membrane o Releases glucose and fructose from sucrose (sugar) so they can be absorbed into the bloodstream PMS 294 2020 QOL Medical, LLC 4 Congenital Sucrase-Isomaltase Deficiency The first report of an autosomal recessive Congenital Sucrase-Isomaltase Deficiency (CSID) was published in 1960. Diarrhoea Caused by Deficiency of Sugar-Splitting Enzymes Weijers HA, Van De Kamer JH, Mossel DAA, Dicke WK. Diarrhoea Caused by Deficiency of Sugar-Splitting Enzymes. Lancet. 1960;276(7145):296-7. PMS 294 2020 QOL Medical, LLC 5 Sucrase-Isomaltase Substrates Sucrose Isomaltose Glucose + Fructose Glucose + Glucose (a-1,2 glycosidic bond) (a-1,6 glycosidic bond) PMS 294 2020 QOL Medical, LLC 6 How Sucrase Works to Hydrolyze Sucrose 1. Enzyme Substrate binds to disaccharide (Sucrose) substrate Enzyme H20 (Sucrase) 4. Active site available for another substrate 3. Products are released and absorbed 2. Substrate is converted to monosaccharides Glucose Fructose PMS 294 2020 QOL Medical, LLC 7 CSID Carb Maldigestion Pathophysiology NORMAL CSID PMS 294 2020 QOL Medical, LLC 8 SI Gene o Encodes a heterodimer with 2 active sites – sucrase and isomaltase • Located on chromosome 31 • Very large – approximately 100 kilobases1 • 48 exons encoding 1827 amino acids1 o 2146 rare variants with 880 SI rare pathogenic variants (SI-RPVs)2 • Sucrase-Isomaltase protein transported and anchored to apical membrane of enterocytes to digest disaccharides in intestinal lumen3 1.
    [Show full text]