Amylase Activity Experiment
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Characterization of Prebiotics and Their Synergistic Activities with Lactobacillus Probiotics for Β-Glucuronidase Reduction
ESEARCH ARTICLE R ScienceAsia 45 (2019): 538–546 doi: 10.2306/scienceasia1513-1874.2019.45.538 Characterization of prebiotics and their synergistic activities with Lactobacillus probiotics for β-glucuronidase reduction a, a b a Achara Chaiongkarn ∗, Jirapa Dathong , Wipaporn Phatvej , Premsuda Saman , Chutima Kuanchaa, Lawan Chatanona, Somporn Moonmungmeea a Biodiversity Research Center, Thailand Institute of Scientific and Technological Research, Pathum Thani 12120 Thailand b Expert Center of Innovative Herbal Products, Thailand Institute of Scientific and Technological Research, Pathum Thani 12120 Thailand ∗Corresponding author, e-mail: [email protected] Received 1 Jun 2018 Accepted 28 Oct 2019 ABSTRACT: The role of synbiotics for enriching health and well-being in addition to suppressing disease is gaining interest. Synergistic activities of four candidate prebiotics as exopolysaccharides (EPSs) derived from Lactobacillus fer- mentum TISTR 2514 (EPS-TISTR 2514), Pediococcus acidilactici TISTR 2612 (EPS-TISTR 2612), manno-oligosaccharides and rice syrup-oligosaccharides were characterized and evaluated for decreasing the risk of colorectal cancer (CRC). Results revealed that one or more candidate prebiotics stimulated the growth of Lactobacillus casei DSM 20011, Lactobacillus plantarum DSM 2648, and Lactobacillus rhamnosus DSM 20021 by at least two orders of magnitude higher than positive control (using FOS as carbon source) within 24 h in vitro. Simulated gastrointestinal (pH 1) and α-amylase (pH 7) resistance were tested. Results showed more than 75% remaining after incubation at 37 °C after 6 h for all treatments except rice syrup. L. plantarum DSM 2648 + manno-oligosaccharides (Tr.1), L. plantarum DSM 2648 + EPS-TISTR 2612 (Tr.2), L. rhamnosus DSM 20021 + rice syrup-oligosaccharides (Tr.3), L. -
Revised Glossary for AQA GCSE Biology Student Book
Biology Glossary amino acids small molecules from which proteins are A built abiotic factor physical or non-living conditions amylase a digestive enzyme (carbohydrase) that that affect the distribution of a population in an breaks down starch ecosystem, such as light, temperature, soil pH anaerobic respiration respiration without using absorption the process by which soluble products oxygen of digestion move into the blood from the small intestine antibacterial chemicals chemicals produced by plants as a defence mechanism; the amount abstinence method of contraception whereby the produced will increase if the plant is under attack couple refrains from intercourse, particularly when an egg might be in the oviduct antibiotic e.g. penicillin; medicines that work inside the body to kill bacterial pathogens accommodation ability of the eyes to change focus antibody protein normally present in the body acid rain rain water which is made more acidic by or produced in response to an antigen, which it pollutant gases neutralises, thus producing an immune response active site the place on an enzyme where the antimicrobial resistance (AMR) an increasing substrate molecule binds problem in the twenty-first century whereby active transport in active transport, cells use energy bacteria have evolved to develop resistance against to transport substances through cell membranes antibiotics due to their overuse against a concentration gradient antiretroviral drugs drugs used to treat HIV adaptation features that organisms have to help infections; they -
NADPH-Dependent A-Oxidation of Unsaturated Fatty Acids With
Proc. Natl. Acad. Sci. USA Vol. 89, pp. 6673-6677, August 1992 Biochemistry NADPH-dependent a-oxidation of unsaturated fatty acids with double bonds extending from odd-numbered carbon atoms (5-enoyl-CoA/A3,A2-enoyl-CoA isomerase/A3',52'4-dienoyl-CoA isomerase/2,4-dienoyl-CoA reductase) TOR E. SMELAND*, MOHAMED NADA*, DEAN CUEBASt, AND HORST SCHULZ* *Department of Chemistry, City College of the City University of New York, New York, NY 10031; and tJoined Departments of Chemistry, Manhattan College/College of Mount Saint Vincent, Riverdale, NY 10471 Communicated by Salih J. Wakil, April 13, 1992 ABSTRACT The mitochondrial metabolism of 5-enoyl- a recent observation of Tserng and Jin (5) who reported that CoAs, which are formed during the (3-oxidation of unsaturated the mitochondrial -oxidation of 5-enoyl-CoAs is dependent fatty acids with double bonds extending from odd-numbered on NADPH. Their analysis of metabolites by gas chroma- carbon atoms, was studied with mitochondrial extracts and tography/mass spectrometry led them to propose that the purified enzymes of (3-oxidation. Metabolites were identified double bond of 5-enoyl-CoAs is reduced by NADPH to yield spectrophotometrically and by high performance liquid chro- the corresponding saturated fatty acyl-CoAs, which are then matography. 5-cis-Octenoyl-CoA, a putative metabolite of further degraded by P-oxidation. linolenic acid, was efficiently dehydrogenated by medium- This report addresses the question of how 5-enoyl-CoAs chain acyl-CoA dehydrogenase (EC 1.3.99.3) to 2-trans-5-cis- are chain-shortened by P-oxidation. We demonstrate that octadienoyl-CoA, which was isomerized to 3,5-octadienoyl- 5-enoyl-CoAs, after dehydrogenation to 2,5-dienoyl-CoAs, CoA either by mitochondrial A3,A2-enoyl-CoA isomerase (EC can be isomerized to 2,4-dienoyl-CoAs, which are reduced by 5.3.3.8) or by peroxisomal trifunctional enzyme. -
Isolated Co-Lipase Deficiency in Two Brothers
Gut: first published as 10.1136/gut.23.3.243 on 1 March 1982. Downloaded from Gut, 1982, 23, 243-246 Case reports Isolated co-lipase deficiency in two brothers H HILDEBRAND,* B BORGSTROM, A BEKASSY, C ERLANSON-ALBERTSSON, AND I HELIN From the Department ofPaediatrics and the Department ofPhysiological Chemistry, University ofLund, Sweden SUMMARY Two normally developed Assyrian brothers with isolated pancreatic co-lipase deficiency are described. They presented at the age of 5-6 years with loose stools. They had steatorrhoea, and analysis of exocrine pancreatic enzymes in the small intestine showed co-lipase deficiency, while amylase, chymotrypsin, trypsin, and lipase were normal. Intraduodenal infusion of purified co-lipase improved fat digestion measured by the triolein breath test. Their steatorrhoea diminished on treatment with enteric-coated pancreatic enzymes. The first indication for the existence of a co-factor for activities were assayed titrimetrically`5 using p-tosyl-l- pancreatic lipase was reported in 1963.1 In 1969 a arginine methyl ester (TAME) and N-acetyl-L-tyro- heat-stable co-factor was separated from lipase by gel- sine ethyl ester (ATEE), respectively, as substrates. filtration.2 Pure pancreatic lipase is inhibited by bile Lipase and co-lipase were measured titrimetrically salts in concentrations over their critical micellar con- using tributyrate as substrate.4 Total bile salt concen- centrations.3 The function of the co-factor, called co- trations and the ratio of glycine- to taurine-conjugated lipase, is to restore -
Chapter 7. "Coenzymes and Vitamins" Reading Assignment
Chapter 7. "Coenzymes and Vitamins" Reading Assignment: pp. 192-202, 207-208, 212-214 Problem Assignment: 3, 4, & 7 I. Introduction Many complex metabolic reactions cannot be carried out using only the chemical mechanisms available to the side-chains of the 20 standard amino acids. To perform these reactions, enzymes must rely on other chemical species known broadly as cofactors that bind to the active site and assist in the reaction mechanism. An enzyme lacking its cofactor is referred to as an apoenzyme whereas the enzyme with its cofactor is referred to as a holoenzyme. Cofactors are subdivided into essential ions and organic molecules known as coenzymes (Fig. 7.1). Essential ions, commonly metal ions, may participate in substrate binding or directly in the catalytic mechanism. Coenzymes typically act as group transfer agents, carrying electrons and chemical groups such as acyl groups, methyl groups, etc., depending on the coenzyme. Many of the coenzymes are derived from vitamins which are essential for metabolism, growth, and development. We will use this chapter to introduce all of the vitamins and coenzymes. In a few cases--NAD+, FAD, coenzyme A--the mechanisms of action will be covered. For the remainder of the water-soluble vitamins, discussion of function will be delayed until we encounter them in metabolism. We also will discuss the biochemistry of the fat-soluble vitamins here. II. Inorganic cation cofactors Many enzymes require metal cations for activity. Metal-activated enzymes require or are stimulated by cations such as K+, Ca2+, or Mg2+. Often the metal ion is not tightly bound and may even be carried into the active site attached to a substrate, as occurs in the case of kinases whose actual substrate is a magnesium-ATP complex. -
Enzymes Main Concepts: •Proteins Are Polymers Made up of Amino Acids
Biology 102 Karen Bledsoe, Instructor Notes http://www.wou.edu/~bledsoek/ Chapter 6, section 4 Topic: Enzymes Main concepts: • Proteins are polymers made up of amino acids. Enzymes are a category of proteins. • Enzymes are catalysts. They speed up the rate of a chemical reaction by reducing the activation energy, which is the energy needed to carry out the reaction. An example of a catalyst: if you put a lit match to a sugar cube, it’s hard to make the sugar catch fire. But if you rub a corner of the sugar cube with ash or charcoal, it catches more easily. The ash or charcoal acts as a catalyst. • Many important chemical reactions in living cells can happen spontaneously, but these reactions happen too rarely and too slowly to sustain life. Enzymes make the reactions happen more quickly and more often. • Some reactions happen too violently to support life. Sugar, when burned, released a lot of energy, but the energy is mostly heat. A rapid reaction like that would overheat our cells. Enzyme-controlled reactions can release energy from sugar in a way that captures most of the energy and loses less of the energy as heat, so that the energy is useful to the cell and does not overheat the cell. • The structure of enzymes allows them to carry out reactions. Each enzyme is shaped to carry out only one specific reaction. This is known as enzyme specificity. Amylase, for example, is an enzyme that breaks down starch into glucose. Amylase only breaks down starch; it does not break down any other molecule, nor does it build starch out of glucose. -
K113436 B. Purpose for Submi
510(k) SUBSTANTIAL EQUIVALENCE DETERMINATION DECISION SUMMARY ASSAY ONLY TEMPLATE A. 510(k) Number: k113436 B. Purpose for Submission: New device C. Measurand: Alkaline Phosphatase, Amylase, and Lactate Dehydrogenase D. Type of Test: Quantitative, enzymatic activity E. Applicant: Alfa Wassermann Diagnostic Technologies, LLC F. Proprietary and Established Names: ACE Alkaline Phosphatase Reagent Amylase Reagent ACE LDH-L Reagent G. Regulatory Information: Product Classification Regulation Section Panel Code CJE II 862.1050, Alkaline phosphatase 75-Chemistry or isoenzymes test system CIJ II 862.1070, Amylase test system 75-Chemistry CFJ II, exempt, meets 862.1440, Lactate 75-Chemistry limitations of dehydrogenase test system exemption. 21 CFR 862.9 (c) (4) and (9) H. Intended Use: 1. Intended use(s): See indications for use below. 2. Indication(s) for use: The ACE Alkaline Phosphatase Reagent is intended for the quantitative determination of alkaline phosphatase activity in serum using the ACE Axcel Clinical Chemistry System. Measurements of alkaline phosphatase are used in the diagnosis and treatment of liver, bone, parathyroid and intestinal diseases. This test is intended for use in clinical laboratories or physician office laboratories. For in vitro diagnostic use only. The ACE Amylase Reagent is intended for the quantitative determination α-amylase activity in serum using the ACE Axcel Clinical Chemistry System. Amylase measurements are used primarily for the diagnosis and treatment of pancreatitis (inflammation of the pancreas). This test is intended for use in clinical laboratories or physician office laboratories. For in vitro diagnostic use only. The ACE LDH-L Reagent is intended for the quantitative determination of lactate dehydrogenase activity in serum using the ACE Axcel Clinical Chemistry System. -
Extrapancreatic Sources of Lipase
Clinical Chemistry Byline David Parry, PhD, FCACB St. Boniface General Hospital James Dalton, PhD, FCACB Health Sciences Centre Extrapancreatic Sources of Lipase Reports now abound in the literature indicating that serum lipase is more specific and sensitive than amylase for detecting acute pancreatitis in patients presenting with acute abdominal pain (1-7). Amylase has been the mainstay biochemical test for the investigation of acute pancreatitis for many years, whereas lipase has not been widely used primarily because, until recently, reliable lipase assays were not suitable for rapid turnaround of results. Now, reliable and rapid lipase results are available at HSC, St. Boniface General Hospital, Seven Oaks General Hospital and Grace General Hospital. It is generally well appreciated that increases in serum amylase are seen not only in pancreatic disorders, but also in a number of non-pancreatic abdominal and non-abdominal diseases (1). With increased use of lipase, it has become increasingly recognized that lipase too can be elevated in clinical conditions that do not involve the pancreas. Even though the superiority of lipase over amylase for investigating acute pancreatitis has been shown repeatedly in recent literature (2-5), it is important to be aware that there are a number of clinical conditions that can give rise to elevated nonpancreatic lipase: 1) A recent study (2) has shown that some patients presenting with acute abdominal pain have elevations in serum lipase that are due to extrapancreatic disease processes. The sources of elevated lipase were attributed to a number of intra-abdominal anatomic locations other than the pancreas, including the biliary tract, esophagus, stomach, duodenum and small intestine. -
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. -
Digestive Enzyme: Amylase
DIGESTIVE ENZYME: AMYLASE BACKGROUND Caution: Most animals begin their digestion in their mouths. Chewing breaks up Lugol’s solution is slightly large pieces of food and chemicals in the saliva begin breaking apart hazardous: molecules of starch. In this experiment we add saliva to crackers to • It should not be observe the how quickly this process begins to happen. handled by small children. Basic definitions: • It is dangerous if Amylase: an enzyme that breaks down starch into sugars. swallowed. Enzyme: a protein that speeds up a chemical reaction. • Participants should Chemical Indicator: a chemical that allows you to observe that a wear gloves. reaction has taken place. • Adults should place Starch: a complex arrangement of sugar molecules. the Lugol’s solution into a small dropper Starch is a long group of glucose (sugar) molecules bonded together. bottle for youth to Amylose is the starch form that’s found in crackers. In amylose, the use. sugar molecules form a structure that has small spaces in between the molecules of sugar. Lugol’s solution contains iodine molecules that fit Skills: tightly inside these small spaces. When the iodine molecules are inside • Observation, these small spaces between bonded sugar molecules, the iodine looks teamwork. blue-black in color. If the sugar molecules begin to break apart and release the iodine molecules, the indicator solution looks light brown- Grade Levels: Grades 4 - brown in color. 12 Amylase is the protein that breaks apart starch into sugars. Amylase is a • Time: 15 – 20 minutes chemical found in the saliva of many animals. Number of Youth: Materials for each test group: Any Lugol’s Solution (2%) in small dropper bottle 2 test tubes with lids : 25ml or 50 ml Supplies Needed: Small cup of water Materials for each test Crushed saltine cracker in zip lock bag group: 5-7 plastic cups: 3 oz. -
The Role of Phospholipase D (Pld) and Grb2 in Chemotaxis
THE ROLE OF PHOSPHOLIPASE D (PLD) AND GRB2 IN CHEMOTAXIS A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science By KATIE J. KNAPEK B.S., Indiana University of Pennyslvania, 2006 2008 Wright State University WRIGHT STATE UNIVERSITY SCHOOL OF GRADUATE STUDIES December 19, 2008 I HEREBY RECOMMEND THAT THE THESIS PREPARED UNDER MY SUPERVISON BY Katie J. Knapek ENTITLED The Role of Phospholipase D (PLD) and Grb2 in Chemotaxis BE ACCEPTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF Master of Science. _____________________________ Julian Gomez-Cambronero, Ph. D. Thesis Director _____________________________ Barbara Hull, Ph. D. Program Director Committee on Final Examination _______________________ Julian Gomez-Cambronero, Ph. D. _______________________ Nancy Bigley, Ph. D. _______________________ Mill Miller, Ph. D. ________________________ Joseph F. Thomas Jr., Ph. D. Dean, School of Graduate Studies ABSTRACT Knapek, Katie J. M.S., Department of Biological Sciences, Microbiology and Immunology Program, Wright State University, 2008. The Role of Phospholipase D (PLD) and Grb2 in Chemotaxis. Phospholipase D (PLD) is an enzyme that hydrolyzes phosphatidylcholine yielding choline and phosphatidic acid. PLD is activated by mitogens (lead to cell division) and motogens (leading to cell migration). PLD is known to contribute to cellular proliferation and deregulated expression of PLD has been implicated in several human cancers. PLD has been found to play a role in leukocyte chemotaxis and adhesion as studied through the formation of chemokine gradients. We have established a model of cell migration comprising three cell lines: macrophages RAW 264.7 and LR-5 (for innate defense), and fibroblast COS-7 cells (for wound healing). -
Enhancement in Phospholipase D Activity As a New Proposed Molecular Mechanism of Haloperidol-Induced Neurotoxicity
International Journal of Molecular Sciences Communication Enhancement in Phospholipase D Activity as a New Proposed Molecular Mechanism of Haloperidol-Induced Neurotoxicity Marek Krzystanek 1,*, Ewa Krzystanek 2 , Katarzyna Skałacka 3 and Artur Pałasz 4 1 Department and Clinic of Psychiatric Rehabilitation, Department of Psychiatry and Psychotherapy, Faculty of Medical Sciences, Medical School of Silesia in Katowice, Ziołowa 45/47, 40-635 Katowice, Poland 2 Department of Neurology, Faculty of Medical Sciences, Medical School of Silesia in Katowice, Medyków 14, 40-772 Katowice, Poland; [email protected] 3 Institute of Psychology, University of Opole, Kopernika 11A Street, 45-040 Opole, Poland; [email protected] 4 Department of Histology, Faculty of Medical Sciences, Medical School of Silesia in Katowice, Medyków 18, 40-752 Katowice, Poland; [email protected] * Correspondence: [email protected] or [email protected] Received: 19 November 2020; Accepted: 1 December 2020; Published: 4 December 2020 Abstract: Membrane phospholipase D (PLD) is associated with numerous neuronal functions, such as axonal growth, synaptogenesis, formation of secretory vesicles, neurodegeneration, and apoptosis. PLD acts mainly on phosphatidylcholine, from which phosphatidic acid (PA) and choline are formed. In turn, PA is a key element of the PLD-dependent secondary messenger system. Changes in PLD activity are associated with the mechanism of action of olanzapine, an atypical antipsychotic. The aim of the present study was to assess the effect of short-term administration of the first-generation antipsychotic drugs haloperidol, chlorpromazine, and fluphenazine on membrane PLD activity in the rat brain. Animals were sacrificed for a time equal to the half-life of the antipsychotic drug in the brain, then the membranes in which PLD activity was determined were isolated from the tissue.