Acute Pancreatitis with Normal Serum Lipase: a Case Series
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Reduction of Pectinesterase Activity in a Commercial Enzyme Preparation
Journal of the Science of Food and Agriculture J Sci Food Agric 85:1613–1621 (2005) DOI: 10.1002/jsfa.2154 Reduction of pectinesterase activity in a commercial enzyme preparation by pulsed electric fields: comparison of inactivation kinetic models Joaquın´ Giner, Pascal Grouberman, Vicente Gimeno and Olga Martın´ ∗ Department of Food Technology, University of Lleida, CeRTA-UTPV, ETSEA, Avda Alcalde Rovira Roure 191, 25198-Lleida, Spain Abstract: The inactivation of pectinesterase (PE) in a commercial enzyme preparation (CEP) under high intensity pulsed electric fields (HIPEF) was studied. After desalting and water dilution of the raw CEP, samples were exposed to exponentially decay waveform pulses for up to 463 µs at electric field intensities ranging from 19 to 38 kV cm−1. Pulses were applied in monopolar mode. Experimental data were fitted to a first-order kinetic model as well as to models based on Fermi, Hulsheger¨ or Weibull equations to describe PE inactivation kinetics. Characteristic parameters for each model were calculated. Relationships between some of the parameters and process variables were obtained. The Weibull model yielded the best accuracy factor. The relationship between residual PE and input of electrical energy density was found to be that of exponential decay. 2005 Society of Chemical Industry Keywords: pulsed electric fields; kinetics; pectinesterase; model; inactivation INTRODUCTION It has become customary to use CEPs in fruit and Pectinesterase (PE; EC 3.1.1.11) is a pectic enzyme vegetable juice technology. Depending -
Understanding Your Blood Test Lab Results
Understanding Your Blood Test Lab Results A comprehensive "Health Panel" has been designed specifically to screen for general abnormalities in the blood. This panel includes: General Chemistry Screen or (SMAC), Complete Blood Count or (CBC), and Lipid examination. A 12 hour fast from all food and drink (water is allowed) is required to facilitate accurate results for some of the tests in this panel. Below, is a breakdown of all the components and a brief explanation of each test. Abnormal results do not necessarily indicate the presence of disease. However, it is very important that these results are interpreted by your doctor so that he/she can accurately interpret the findings in conjunction with your medical history and order any follow-up testing if needed. The Bernards Township Health Department and the testing laboratory cannot interpret these results for you. You must speak to your doctor! 262 South Finley Avenue Basking Ridge, NJ 07920 www.bernardshealth.org Phone: 908-204-2520 Fax: 908-204-3075 1 Chemistry Screen Components Albumin: A major protein of the blood, albumin plays an important role in maintaining the osmotic pressure spleen or water in the blood vessels. It is made in the liver and is an indicator of liver disease and nutritional status. A/G Ratio: A calculated ratio of the levels of Albumin and Globulin, 2 serum proteins. Low A/G ratios can be associated with certain liver diseases, kidney disease, myeloma and other disorders. ALT: Also know as SGPT, ALT is an enzyme produced by the liver and is useful in detecting liver disorders. -
Download Product Insert (PDF)
PRODUCT INFORMATION Lysophospholipase D Polyclonal Antibody Item No. 10005375 Overview and Properties Contents: This vial contains 500 µl of peptide affinity-purified antibody. Synonyms: Autotaxin, ENPP2, lysoPLD Immunogen: Peptide from the C-terminal region of rat LysoPLD Species Reactivity: (+) Human, mouse, and rat; other species not tested Form: Liquid Storage: -20°C (as supplied) Stability: ≥1 year Storage Buffer: TBS, pH 7.4, with 50% glycerol, 0.1%l BSA, and 0.02% sodium azide Host: Rabbit Applications: Immunocytochemistry (ICC), Immunohistochemistry (IHC), and Western blot (WB); the recommended starting dilution for ICC is 1:500, 1:80 for IHC, and 1:200 for WB. Other applications were not tested, therefore optimal working concentration/dilution should be determined empirically. Images 1 · · · · · · · 104 kDa · · · · · · · 60 kDa Lane 1: Human cerebella supernatant (40 µg) Immunohistochemistry analysis of formalin-fixed, paraffin-embedded (FFPE) human cerebellum ǎssue aer heat-induced anǎgen retrieval in pH 6.0 citrate buffer. Aer incubaǎon with Lysophospholipase D Polyclonal Anǎbody (Item No. 10005375) at a 1:80 diluǎon, slides were incubated with bioǎnylated secondary anǎbody, followed by alkaline phosphatase-strepavidin and chromogen (DAB). WARNING CAYMAN CHEMICAL THIS PRODUCT IS FOR RESEARCH ONLY - NOT FOR HUMAN OR VETERINARY DIAGNOSTIC OR THERAPEUTIC USE. 1180 EAST ELLSWORTH RD SAFETY DATA ANN ARBOR, MI 48108 · USA This material should be considered hazardous until further information becomes available. Do not ingest, inhale, get in eyes, on skin, or on clothing. Wash thoroughly after handling. Before use, the user must review the complete Safety Data Sheet, which has been sent via email to your institution. PHONE: [800] 364-9897 WARRANTY AND LIMITATION OF REMEDY [734] 971-3335 Buyer agrees to purchase the material subject to Cayman’s Terms and Conditions. -
Ionized Calcium: Analytical Challenges and Clinical Relevance
16 Review Article Page 1 of 16 Ionized calcium: analytical challenges and clinical relevance Aghilès Hamroun1, Jean-David Pekar2, Arnaud Lionet1, Amjad Ghulam3, Patrice Maboudou2, Ambroise Mercier2, Thierry Brousseau2, Guillaume Grzych3,4, François Glowacki1,5 1CHU Lille, Service de Néphrologie, F-59000, Lille, France; 2CHU Lille, Biochimie Automatisée (UF-8832), Pôle de Biologie Pathologie Génétique, F-59000, Lille, France; 3CHU Lille, Service « Hormonologie, Métabolisme, Nutrition, Oncologie », Pôle de Biologie Pathologie Génétique, Lille, France; 4INSERM, U1011-EGID, Institut Pasteur de Lille, F-59000, Lille, France; 5EA 4483-IMPECS-IMPact of Environmental Chemicals on Human Health, Research Department, 59045, Lille, France Contributions: (I) Conception and design: G Grzych, JD Pekar, A Hamroun; (II) Administrative support: G Grzych, JD Pekar, A Hamroun; (III) Provision of study materials or patients: None; (IV) Collection and assembly of data: G Grzych, JD Pekar, A Hamroun; (V) Data analysis and interpretation: G Grzych, JD Pekar, A Hamroun; (VI) Manuscript writing: All authors; (VII) Final approval of manuscript: All authors. Correspondence to: Dr. Guillaume Grzych, MD, MSc. Laboratory of Biochemistry, Biology and Pathology Center, Lille University Hospital, Pr J. Leclercq Boulevard, 59037 Lille, France. Email: [email protected]. Abstract: Calcium is a central electrolyte involved in many physiological functions commonly measured in clinical practice. Abnormal calcium levels are frequently found, and could have serious clinical consequences. The free form of calcium, also called ionized calcium, plays a determining role in the human body. Its measurement still remains limited by technical, analytical and financial constraints. To overcome these limits, many formulas have been developed to estimate the ionized calcium value. -
Diagnostic Value of Serum Enzymes-A Review on Laboratory Investigations
Review Article ISSN 2250-0480 VOL 5/ ISSUE 4/OCT 2015 DIAGNOSTIC VALUE OF SERUM ENZYMES-A REVIEW ON LABORATORY INVESTIGATIONS. 1VIDYA SAGAR, M.SC., 2DR. VANDANA BERRY, MD AND DR.ROHIT J. CHAUDHARY, MD 1Vice Principal, Institute of Allied Health Sciences, Christian Medical College, Ludhiana 2Professor & Ex-Head of Microbiology Christian Medical College, Ludhiana 3Assistant Professor Department of Biochemistry Christian Medical College, Ludhiana ABSTRACT Enzymes are produced intracellularly, and released into the plasma and body fluids, where their activities can be measured by their abilities to accelerate the particular chemical reactions they catalyze. But different serum enzymes are raised when different tissues are damaged. So serum enzyme determination can be used both to detect cellular damage and to suggest its location in situ. Some of the biochemical markers such as alanine aminotransferase, aspartate aminotransferase, alkaline phasphatase, gamma glutamyl transferase, nucleotidase, ceruloplasmin, alpha fetoprotein, amylase, lipase, creatine phosphokinase and lactate dehydrogenase are mentioned to evaluate diseases of liver, pancreas, skeletal muscle, bone, etc. Such enzyme test may assist the physician in diagnosis and treatment. KEYWORDS: Liver Function tests, Serum Amylase, Lipase, CPK and LDH. INTRODUCTION mitochondrial AST is seen in extensive tissue necrosis during myocardial infarction and also in chronic Liver diseases like liver tissue degeneration DIAGNOSTIC SERUM ENZYME and necrosis². But lesser amounts are found in Enzymes are very helpful in the diagnosis of brain, pancreas and lung. Although GPT is plentiful cardiac, hepatic, pancreatic, muscular, skeltal and in the liver and occurs only in the small amount in malignant disorders. Serum for all enzyme tests the other tissues. -
What Is Alkaline Phosphatase? What Are the Symptoms of Low ALP?
What is the treatment for HPP? In 2015, asfotase alfa (Strensiq™) was approved for use in the US, the European Union, and Canada for pediatric-onset HPP, and in Japan for HPP with onset at any age. The medication is an injection given multiple times per week underneath the skin (subcutaneous). It is a recombinant (factory-made) form of ALP that has a bone-targeting component. When patients take asfotase alfa, ALP levels measured in the blood are quite high (often in the multiple thousands). Therefore, measuring ALP levels is typically not helpful once a patient is on therapy. What is Alkaline Phosphatase? What are the symptoms of low ALP? For more information, please contact Patients with hypophosphatasia (HPP) have Low ALP can lead to multiple symptoms of HPP, the Soft Bones Foundation. a low blood alkaline phosphatase (ALP) level. including poor bone mineralization and rickets as well (866) 827-9937 – Toll Free as early tooth loss (prior to age 5 years). It is also (973) 453-3093 – Direct Line thought that PPi may build up in muscle tissue 121 Hawkins Place, #267 ALP is an enzyme (a protein that breaks down and may be responsible for the pain and muscle Boonton, New Jersey 07005 chemicals). Most health providers are aware that weakness that some patients with HPP experience. www.SoftBones.org high ALP levels may indicate medical problems, such as liver disease or other bone diseases besides HPP, but many providers may not recognize that low ALP levels can indicate HPP. Low ALP is important What questions should patients ask Written by because the inability to break down chemicals can their doctors about ALP? Jill Simmons, MD lead to elevated levels of these chemicals, which Associate Professor of Pediatrics, Ian Burr Division can cause multiple problems. -
Medical Tests
Waldenstrom’s Macroglobulinemia Medical Tests WALDENSTROM’S MACROGLOBULINEMIA MEDICAL TESTS The IWMF Vision Statement A World Without WM (Waldenstrom's macroglobulinemia). The IWMF Mission Statement Support and educate everyone affected by Waldenstrom's macroglobulinemia (WM) while advancing the search for a cure. To accomplish this vision, the IWMF offers WM patients, caregivers, family members, and friends six invaluable services: • Information from our website and our publications written in a patient-friendly way to promote understanding of our rare disease • Education at our annual Educational Forum to help patients and caregivers learn about our disease from WM researchers and clinicians • On-going updates about WM and the IWMF sent through our quarterly IWMF Torch magazine and our NEWS releases • Peer support from others who’ve been where you are • Information for medical professionals who may have limited experience with our rare disease • Research directed to better treatments while we search for a cure Since WM is a rare disease, the IWMF relies upon individuals for financial support and upon volunteers to do much of its work. Published by the International Waldenstrom’s Macroglobulinemia Foundation (IWMF) This information has been provided by the IWMF at no cost to you. Please consider Joining and/or contributing to the IWMF to enable us to continue to provide materials like this to support research toward better treatments and a cure for Waldenstrom’s macroglobulinemia. You may Join and/or contribute at our website, www.iwmf.com, or you may mail your contribution to: 6144 Clark Center Avenue, Sarasota, FL 34238. IWMF is a 501(c)(3) Tax Exempt Non-Profit Organization, Fed ID #54-1784426. -
Effect of Alkaline Phosphatase on the Function of Purified Reverse Transcriptase in Reconstructed Reverse Transcription (116 Pp) Director: Kenneth F
University of Montana ScholarWorks at University of Montana Graduate Student Theses, Dissertations, & Professional Papers Graduate School 1984 Effect of alkaline phosphatase on the function of purified er verse transcriptase in reconstructed reverse transcription Michael J. Wolkowicz The University of Montana Follow this and additional works at: https://scholarworks.umt.edu/etd Let us know how access to this document benefits ou.y Recommended Citation Wolkowicz, Michael J., "Effect of alkaline phosphatase on the function of purified er verse transcriptase in reconstructed reverse transcription" (1984). Graduate Student Theses, Dissertations, & Professional Papers. 7480. https://scholarworks.umt.edu/etd/7480 This Thesis is brought to you for free and open access by the Graduate School at ScholarWorks at University of Montana. It has been accepted for inclusion in Graduate Student Theses, Dissertations, & Professional Papers by an authorized administrator of ScholarWorks at University of Montana. For more information, please contact [email protected]. COPYRIGHT ACT OF 1976 This is an unpublished manuscript in which copyright sub s i s t s . Any further reprinting of its contents must be approved BY THE a u t h o r . Mansfield Library University of Montana Date ; 1 G 8 5 EFFECT OF ALKALINE PHOSPHATASE ON THE FUNCTION OF PURIFIED REVERSE TRANSCRIPTASE IN RECONSTRUCTED REVERSE TRANSCRIPTION By Michael J. Wolkowicz B. A. American International College, 1976 B. S. University of Montana, 1980 Presented in partial fulfillment of the requirements for the degree of Masters of Science UNIVERSITY OF MONTANA 1984 Approved by: iP- airman. Board of Examiners D^n, Graduater'school Date UMI Number: EP38281 All rights reserved INFORMATION TO ALL USERS The quality of this reproduction is dependent upon the quality of the copy submitted. -
The Characterization of Oligonucleotides and Nucleic Acids Using Ribonuclease H and Mass Spectrometry
Louisiana State University LSU Digital Commons LSU Historical Dissertations and Theses Graduate School 1999 The hC aracterization of Oligonucleotides and Nucleic Acids Using Ribonuclease H and Mass Spectrometry. Lenore Marie Polo Louisiana State University and Agricultural & Mechanical College Follow this and additional works at: https://digitalcommons.lsu.edu/gradschool_disstheses Recommended Citation Polo, Lenore Marie, "The hC aracterization of Oligonucleotides and Nucleic Acids Using Ribonuclease H and Mass Spectrometry." (1999). LSU Historical Dissertations and Theses. 6923. https://digitalcommons.lsu.edu/gradschool_disstheses/6923 This Dissertation is brought to you for free and open access by the Graduate School at LSU Digital Commons. It has been accepted for inclusion in LSU Historical Dissertations and Theses by an authorized administrator of LSU Digital Commons. For more information, please contact [email protected]. INFORMATION TO USERS This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter free, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction. 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 copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand corner and continuing from left to right in equal sections with small overlaps. -
Lipase Interpretive Summary
Lipase Interpretive Summary Description: Lipase is an enzyme produced primarily in the pancreas to break down dietary fats in the small intestine. Decreased Lipase Common Causes Artifact o Hemolysis directly inhibits lipase activity in the assay Decreased lipase is not clinically significant. Increased Lipase Common Causes Pancreatic acinar cell damage o Inflammation o Necrosis o Neoplasia o Pancreatic duct obstruction Gastrointestinal inflammation Decreased renal clearance/inactivation (any condition that reduces glomerular filtration rate [GFR]) o Pre-renal conditions . Shock . Dehydration . Poor cardiac output o Renal disease o Post-renal disorders . Urinary tract obstruction or rupture Glucocorticoid treatment Uncommon Causes Hepatic neoplasia (dogs) Peritonitis Bowel obstruction Widespread steatitis Related Findings Pancreatic acinar cell damage o Increased amylase o Increased Spec cPL®/Spec fPL®. o Increased ALP +/- bilirubin o Increased glucose o Inflammatory leukogram on CBC Gastrointestinal inflammation o Increased BUN with gastric bleeding Decreased renal clearance/inactivation o Pre-renal . Increased hematocrit and total protein Generated by VetConnect® PLUS: Lipase Page 1 of 2 . Increased BUN, creatinine, and possibly phosphorous . Increased urine specific gravity . Decreased blood pressure (shock, poor cardiac output) o Renal . Increased BUN, creatinine, phosphorus . Isosthenuria o Post-renal . Increased BUN, creatinine, and possibly phosphorus . Abnormalities on urinalysis (blood, inflammation, crystals, etc.) . Abnormalities associated with urinary tract obstruction/rupture on abdominal ultrasound or contrast studies Additional Information Physiology Lipase is a cytoplasmic enzyme produced by the pancreas and released into the small intestine to catalyze the hydrolysis of triglycerides for absorption into the lacteals and gastrointestinal blood vessels. In addition to pancreatic acinar cells, lipase is produced by gastric mucosal cells, hepatocytes, and many extrahepatic cells (including adipocytes and myocytes). -
Regulation of Fructose-6-Phosphate 2-Kinase By
Proc. Natt Acad. Sci. USA Vol. 79, pp. 325-329, January 1982 Biochemistry Regulation of fructose-6-phosphate 2-kinase by phosphorylation and dephosphorylation: Possible mechanism for coordinated control of glycolysis and glycogenolysis (phosphofructokinase) EISUKE FURUYA*, MOTOKO YOKOYAMA, AND KOSAKU UYEDAt Pre-Clinical Science Unit of the Veterans Administration Medical Center, 4500 South Lancaster Road, Dallas, Texas 75216; and Biochemistry Department of the University ofTexas Health Science Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235 Communicated by Jesse C. Rabinowitz, September 28, 1981 ABSTRACT The kinetic properties and the control mecha- Fructose 6-phosphate + ATP nism of fructose-6-phosphate 2-kinase (ATP: D-fructose-6-phos- -3 Fructose + ADP. [1] phate 2-phosphotransferase) were investigated. The molecular 2,6-bisphosphate weight of the enzyme is -100,000 as determined by gel filtration. The plot of initial velocity versus ATP concentration is hyperbolic We have shown that the administration of extremely low con- with a K. of 1.2 mM. However, the plot of enzyme activity as a centrations of glucagon (0.1 fM) or high concentrations of epi- function of fructose 6-phosphate is sigmoidal. The apparent K0.5 nephrine (10 ,uM) to hepatocytes results in inactivation offruc- for fructose 6-phosphate is 20 ,IM. Fructose-6-phosphate 2-kinase tose-6-phosphate 2-kinase and concomitant decrease in the is inactivated by -the catalytic subunit of cyclic AMP-dependent fructose 2,6-bisphosphate level (12). These results, as well as protein kinase, and the inactivation is closely correlated with phos- more recent data using Ca2+ and the Ca2+ ionophore A23187 phorylation. -
Simple, Sensitive Detection of Protein Phosphodiesterase Activity Measure Real-Time Signal Differences in the Picomole Range with the Phosphate Sensor Method
APPLICATION NOTE Phosphodiesterase Activity: A Phophate Sensor Application Simple, Sensitive Detection of Protein Phosphodiesterase Activity Measure real-time signal differences in the picomole range with the Phosphate Sensor method Described in this application is a method utilizing the Life Technologies Phosphate Sensor, a simple tool to interrogate the activity of phosphate-releasing enzymes. The assays described detect the increase of fluorescence intensity when free inorganic phosphate binds to a bacterially derived phosphate-binding protein modified with a fluorophore.To evaluate the Phosphate Sensor methods, we compared detection by coupling to an alkaline phosphatase against a commonly used coupled luciferase assay, examined responses for human phosphodiesterase A (PTE5A) in a titration, in real-time kinetic mode, and with a sildenafil citrate inhibitor. Phosphate Sensor is orders of magnitude more sensitive than the coupled luciferase method, faster and simpler to use than other competitor methods, and uniquely qualified for determining enzymatic rates. Second messenger systems that involve an increase or decrease of cyclic nucleotides (cAMP or cGMP) mediate intracellular signal trans- duction. Nucleotide degradation regulates this process and is mediated through the action of phosphodiesterase (PDE) enzymes, which also play an integral role in a number of disorders including erectile dysfunction [1], asthma [2], and chronic obstructive pulmonary disease [2], as well as schizophrenia, bipolar disorder, and major depression [3]. As research identifies additional potential drug targets, methodologies for measur- ing activity become vital. Figure 1. Phosphate Sensor assay principle. The protein ribbon diagram illustrates the modified We describe here the use and optimization of a simple, flexible reagent phosphate-binding protein with the MDCC fluoro- for measurement of phosphodiesterase activity through coupling it with phore (shown in blue).