نتایج جستجو برای: group ii phospholipases a2

تعداد نتایج: 1517520  

Journal: :Frontiers in Plant Science 2019

Journal: :American journal of physiology. Gastrointestinal and liver physiology 2001
R A Rozenfeld X Liu I DePlaen W Hsueh

We previously showed that group II phospholipase A2 (PLA2-II), a secretory, bactericidal, and proinflammatory protein in intestinal crypts, is upregulated after lipopolysaccharide (LPS) and platelet-activating factor (PAF) challenge. Here we examined whether germ-free environment (GF) or antibiotic treatment (ABX) affects the pathophysiological responses and intestinal PLA2-II activity after PA...

Journal: :Gut 1994
T Minami H Tojo Y Shinomura Y Matsuzawa M Okamoto

The immunochemical protein content of group II phospholipase A2 (PLA2) and PLA2 enzymatic activity were measured for colonic mucosal biopsy samples obtained from patients with either Crohn's disease of the colon or ulcerative colitis, and control patients without inflammatory bowel disease. Immunoreactive group II PLA2 (IR-PLA2 II) content and PLA2 activity in actively inflamed colonic mucosa o...

Journal: :The Journal of biological chemistry 1990
G W Wright C E Ooi J Weiss P Elsbach

A granule-associated phospholipase A2 from rabbit polymorphonuclear leukocytes and a closely similar phospholipase A2 from rabbit serum have been purified to near homogeneity by ion-exchange and reverse-phase chromatography. The cellular (polymorphonuclear leukocyte) phospholipase A2 has been purified greater than 100,000-fold and the extracellular (serum) phospholipase A2 approximately 60,000-...

Journal: :Biochemical Society transactions 1994
A R Kinkaid D C Wilton

The human group II secretory phospholipase A, (sPLA,) has been implicated in a number of inflammatory conditions, including rheumatoid arthritis. A continuous fluorescence displacement assay which measures the release of long chain fatty acids [l] has been used to investigate the activity of a recombinant form of this human enzyme (HR PLAJ and is reported here for the first time. Secretory phos...

Journal: :The Journal of biological chemistry 1988
W Cho A G Tomasselli R L Heinrikson F J Kézdy

A basic monomeric phospholipase A2 from the venom of the American water moccasin, Agkistrodon piscivorus piscivorus, undergoes Ca2+-dependent, autocatalytic acylation during the course of hydrolysis of both model and natural phospholipid substrates. Acylation occurs at 2 lysine residues, Lys-7 and Lys-10, in the NH2-terminal alpha-helical segment of the enzyme, and when both positions are fully...

2014
C. L. S. Guimarães S. H. Andrião-Escarso L. S. Moreira-Dill B. M. A. Carvalho D. P. Marchi-Salvador N. A. Santos-Filho C. A. H. Fernandes M. R. M. Fontes J. R. Giglio B. Barraviera J. P. Zuliani C. F. C. Fernandes L. A. Calderón R. G. Stábeli F. Albericio S. L. da Silva A. M. Soares

Crude venom of Bothrops jararacussu and isolated phospholipases A2 (PLA2) of this toxin (BthTX-I and BthTX-II) were chemically modified (alkylation) by p-bromophenacyl bromide (BPB) in order to study antibody production capacity in function of the structure-function relationship of these substances (crude venom and PLA2 native and alkylated). BthTX-II showed enzymatic activity, while BthTX-I di...

Journal: :The Journal of biological chemistry 1980
J Prigent-Dachary M C Boffa M R Boisseau J Dufourcq

The interaction of snake venom phospholipases A2 with phospholipids has been studied by intrinsic fluorescence. This has been performed in order to understand why some enzymes possess anticoagulant properties while others have no action on blood clotting. We show that phospholipases A2 can be distinguished according to their binding properties to phospholipid vesicles. Strong inhibitors of coag...

2014
Catherine A. Vulfius Igor E. Kasheverov Vladislav G. Starkov Alexey V. Osipov Tatyana V. Andreeva Sergey Yu. Filkin Elena V. Gorbacheva Maxim E. Astashev Victor I. Tsetlin Yuri N. Utkin

Phospholipases A2 represent the most abundant family of snake venom proteins. They manifest an array of biological activities, which is constantly expanding. We have recently shown that a protein bitanarin, isolated from the venom of the puff adder Bitis arietans and possessing high phospholipolytic activity, interacts with different types of nicotinic acetylcholine receptors and with the acety...

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