نتایج جستجو برای: proteinases

تعداد نتایج: 2966  

Journal: :European journal of biochemistry 2004
Isaura Simões Carlos Faro

Aspartic proteinases of the A1 family are widely distributed among plant species and have been purified from a variety of tissues. They are most active at acidic pH, are specifically inhibited by pepstatin A and contain two aspartic residues indispensible for catalytic activity. The three-dimensional structure of two plant aspartic proteinases has been determined, sharing significant structural...

Journal: :The Journal of biological chemistry 2007
Maureen J Gorman Yang Wang Haobo Jiang Michael R Kanost

Melanization, an insect immune response, requires a set of hemolymph proteins including pathogen recognition proteins that initiate the response, a cascade of mostly unknown serine proteinases, and phenoloxidase. Until now, only initial and final proteinases in the pathways have been conclusively identified. Four such proteinases have been purified from the larval hemolymph of Manduca sexta: he...

Journal: :Investigative ophthalmology & visual science 1993
S S Twining S E Kirschner L A Mahnke D W Frank

PURPOSE To determine the effects of exoproducts from the corneal pathogen Pseudomonas aeruginosa on corneal proteinases and proteins. METHODS Whole rabbit corneas were cultured in the presence or absence of broths conditioned with Pseudomonas aeruginosa, elastase, alkaline protease, and exotoxin A. Protein synthesis was assayed by adding 35S-methionine during the last 6 hours of culture. Case...

Journal: :Journal of immunology 2002
Danqing Min Anthony G Moore Michael A Bain Samuel N Breit J Guy Lyons

LPS induces an up-regulation of promatrix metalloproteinase-9 (proMMP9) gene expression in cells of the monocyte/macrophage lineage. We demonstrate here that LPS preparations are also able to activate proMMP9 made by human macrophages or THP-1 cells via LPS-associated proteinases, which cleave the N-terminal propeptide at a site or sites close to the one cleaved upon activation with organomercu...

Journal: :Frontiers in bioscience : a journal and virtual library 2006
Fengyu Song Kessiri Wisithphrom Jing Zhou L Jack Windsor

Cleavage of the fibrillar collagens occurs during physiological conditions, as well as pathological conditions. The resistance of the fibrillar collagens to degradation is due to their rigid and compact structures. There are only a limited number of proteinases that have the capability to initiate the cleavage of the fibrillar collagens. These include some of the matrix metalloproteinases (MMPs...

2006
Daisuke Yamauchi

Storage proteins in cotyledons of legume plants are degraded by proteinases after germination. We examined whether abscisic acid (ABA), gibberellin (GA) and brassinosteroid (BR) are involved in the expression of cysteine proteinases in cotyledons of common bean seeds with RNA blotting using cDNAs for five papain-like proteinases, EP-C1, CP1, CP2, CP3, CP4 and two legumain-like proteinases, LLP1...

Journal: :Cancer research 1985
S Zucker R M Lysik J Wieman D P Wilkie B Lane

In this study we have examined the tissue-destructive proteinases of human pancreatic ductal cancer cell lines derived initially from xenogenic transplants. Cancer cell organelles were isolated following nitrogen cavitation using sucrose density gradient centrifugation. Serine, cysteine, and metalloproteinases were assayed using radiolabeled protein and synthetic substrates. Tumor-induced RBC l...

Journal: :The Journal of biological chemistry 1997
T Okamoto T Akaike M Suga S Tanase H Horie S Miyajima M Ando Y Ichinose H Maeda

Matrix metalloproteinases (MMPs) are zinc-containing proteinases that participate in tissue remodeling under physiological and pathological conditions. To test the involvement of bacterial proteinases in tissue injury during bacterial infections, we investigated the activation potential of various bacterial proteinases against precursors of MMPs (proMMPs) purified from human neutrophils (proMMP...

Journal: :Biochimie 2010
Steven T Olson Benjamin Richard Gonzalo Izaguirre Sophia Schedin-Weiss Peter G W Gettins

Serpin family protein proteinase inhibitors regulate the activity of serine and cysteine proteinases by a novel conformational trapping mechanism that may itself be regulated by cofactors to provide a finely-tuned time and location-dependent control of proteinase activity. The serpin, antithrombin, together with its cofactors, heparin and heparan sulfate, perform a critical anticoagulant functi...

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