3 edition of The action of pancreatic lipase on lipid monolayers found in the catalog.
The action of pancreatic lipase on lipid monolayers
Written in English
|Statement||by James W. Lagocki.|
|LC Classifications||Microfilm 40007 (Q)|
|The Physical Object|
|Pagination||vii, 142 leaves|
|Number of Pages||142|
|LC Control Number||88893353|
Brockerhoff, H.: Action of Pancreatic Lipase on Emulsions of Water-Insoluble Esters, Arch Biochem Biophys , , Brockerhoff, H.: Esters of Phenols as Substrate for Pancreatic Lipase, Biochim Biophys Acta , , Bengt Borgström, The action of bile salts and other detergents on pancreatic lipase and the interaction with colipase, Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, /(77), , 3, (), ().(75)X.
We also studied a lipase from Pseudomonas fluorescens (PFL) because this is a typical bacterium of refngerated milk (3) (6). So thé interactions of porcine pancreatic lipase, milk lipoprotein lipase and lipase from Pseudomonas fluorescens with milk fat globule membrane (MFGM) monolayers hâve been compared using a Langmuir :// Lindstrom, M., Sternby, B., and Borgström, B., , concerted action of human carboxyl ester lipase and pancreatic lipase during digestion in vitro:Importance of the physiochemical state of the substrate, PubMed CrossRef Google Scholar
lipid/water interface. Lipid monolayers have been used as substrates for lipolytic enzymes for over 50 years. This highly sensitive technique and III’ were generated in situ and extemporaneously by the action of the porcine pancreatic lipase (PPL)’ on monomolecular films compounds II and III, respectively, as described below. Lipoprotein lipase: mechanism of action and role in lipoprotein metabolism. Quinn D, Shirai K, Jackson RL Prog Lipid Res, 22(1), 01 Jan
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1. J Am Chem Soc. May 6;92(9) Kinetic analysis of the action of pancreatic lipase on lipid monolayers. Lagocki JW, Boyd NM, Law JH, Kézdy :// Kinetic analysis of the action of pancreatic lipase on lipid monolayers. James W. Lagocki, Norman D. Boyd The surface pressure dependency of the enzymatic hydrolysis of lipid monolayers enzyme denaturation at the air-water interface.
Effect of surface pressure on the hydrolysis of ester monolayers by pancreatic lipase. Biochimica et Colipase is a cofactor protein which forms a complex with pancreatic lipase. This facilitates lipase adsorption to phosphatidylcholine-rich interfaces, presumably as a consequence of the higher affinity of colipase for such interfaces.
According to this model, the presence of colipase in an interface should be sufficient to enable lipase adsorption from the aqueous phase. To test this Action of a microbial lipase/acyltransferase on phospholipid monolayers.
Biochemistry30 (24), DOI: /bia Akio Sugihara, Youssef Gargouri, Gerard Pieroni, Claude Riviere, Louis Sarda, and Robert :// Pancreatic Lipase. Pancreatic triacylglycerol lipase is the single most important determinant of lipid absorption.
In its absence, only 30% of an ingested lipid load is absorbed. The enzyme is secreted by the acinar glands of the pancreas into the pancreatic duct and then into the intestine in /agricultural-and-biological-sciences/pancreatic-lipase.
During the action of pancreatic lipase and colipase on racemic 1,2-didodecanoylglycerol monolayers in the absence of bile salts, biphasic kinetics was observed under conditions of high lipid packing.
Similar kinetics has earlier been reported using phospholipid-emulsified triolein droplets (Borgström, B.
() Gastroenterol ). During the action of pancreatic lipase and colipase on racemic 1,2-didodecanoylglycerol monolayers in the absence of bile salts, biphasic kinetics was observed under conditions of high lipid packing.
Similar kinetics has earlier been reported using phospholipid-emulsified triolein droplets. These kinetics are characterized by a lag time τ(d), dependent on products accumulation at the Adsorption and Activation of Pancreatic Lipase at Interfaces.
Chapus, M. Semeriva, M. Charles, P. Desnuelle Mode of Action of Pancreatic Colipase. Bengt Borgström. Pages Studies of Lipase and Phospholipase A 2 Acting on Lipid Monolayers.
Verger, J. Rietsch, F. Pattus, F. Ferrato, G. Pieroni, G. De Haas et al Pancreatic lipase exhibits optimal activity under alkaline conditions and hydrolyzes triglycerides to fatty acids and glycerol, but mono- and diglycerides are also end products.
Pancreatic lipase has greater activity against short-chain than long-chain triglycerides (Cohen et al., ). Phospholipases A and B also are present in pancreatic :// /pancreatic-lipase. The interaction of the pancreatic lipase cofactor colipase with a diacylphosphatidylcholine, acylglycerols, and free fatty acid was investigated by monitoring its adsorption to monomolecular lipid films.
Surface pressure and colipase surface concentration were measured as a function of the initial lipid concentration and composition. Colipase adsorbs to a level of 28−30 pmol/cm2 to form a The Kinetic Study of Enzyme Action on Substrate Monolayers PASCREATIC LIPASE lUXACTIONS* (Received for publication, Aug ) JAAIES W.
LAGOCKI,~ JOHN H. LAW, AND FERENC J. E&DY From the Department of Biochemistry, The University of Chicago,Illinois SUMMARY The enzymatic reaction of porcine pancreatic lipase The chemical composition of the interface at which a lipase functions in vivo is determined by the local environment.
A general rule is, however, that, prior to lipolysis, the particle interface will be composed predominantly of the more amphipathic constituents of the local milieu and, depending on their exchangeability, constituents of the site at which the lipid particle was :// Momsen, W.
and Brockman, H. () The adsorption to and hydrolysis of 1,3-didecanoyl glycerol monolayers by pancreatic lipase. Effect of substrate packing density. Biol. Chem.– PubMed Google Scholar [14C]DDT was absorbed into mixed lipid micelles during the digestion of olive oil by pancreatic lipase.
Taurocholic acid and [14C]DDT combined together forming a mixed micelle was shown by The equations of Mass Action kinetics are less successful. Equivalent data on the lipolysis of didodecanoyl phosphatidylglycerol by pancreatic lipase can also be interpreted by arguing that the adsorbed enzyme forms significant amounts of enzyme substrate complex which reacts to give products in accordance with the well-known Briggs-Haldane The turkey pancreatic lipase (TPL) was purified from delipidated pancreases.
This avian pancreatic lipase contains amino acids and presents an experimental mass of 49, Da. To investigate the structure-function relationships of this lipase, TPL was expressed in Pichia :// Action.
Lipoprotein Lipase on Mixed determine the rate of hydrolysis of lipid monolayers at constant. were obtained with pancreatic lipase using mixed lipid mono- layers.
as Chitosan does not inhibit enzymatic action of human pancreatic lipase in Langmuir monolayers of 1,2-didecanoyl-glycerol (DDG). Souza AL, Pavinatto FJ, Caseli L, Volpati D, Miranda PB, Oliveira ON Jr Colloids Surf B Biointerfaces Nov 1; The β5‘ Loop of the Pancreatic Lipase C2-like Domain Plays a Critical Role in the Lipase−Lipid Interactions.
Biochemistry41 (46), DOI: /bi Mustapha Aoubala, Margarita Ivanova, Isabelle Douchet, Alain De Caro, and Robert :// Hydrolysis Rates of Phospholipid Monolayers by Pancreatic Lipase-De Haas et al. (19) reported in that pure pancreatic lipase in the presence of bile salts hydrolyzed ester bonds in position 1 of egg lecithin.
Later, Slotboom et al. (20, 21) confirmed and. Action of Lipase on Substrate Monolayers. The Mechanism of Lipase Action as Studied with Soluble Substrates and Inert Interfaces.
The Lipase–Colipase System. Interactions among Lipase, Colipase, and Bile Salts in Aqueous Solution. Chemical Labeling of Lipase The purpose of the present work is to discuss some properties of two pancreatic proteins, lipase and colipase, involved in the intraduodenal digestion of dietary fat.
Lipase has been known for a number of years to catalyse with other digestive enzymes the conversion Biochimica et Biophysica Acta, () Elsevier Scientific Publishing Company, Amsterdam - Printed in The Netherlands BBA EFFECT OF SURFACE PRESSURE ON THE HYDROLYSIS OF ESTER MONOLAYERS BY PANCREATIC LIPASE S.
ESPOSITO, M. SI~Mt~RIVA AND P. DESNUELLE Institut de Chimie Biologique, Universitd de Provence, Place V. Hugo, 13