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Proteolytic enzymes

About: Proteolytic enzymes is a research topic. Over the lifetime, 23096 publications have been published within this topic receiving 835544 citations.


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Journal ArticleDOI
TL;DR: An enzyme that hydrolyzes di-N-acetylchitobiose linkages in oligosaccharides and glycoproteins was purified to homogeneity from cultural filtrates of Streptomyces griseus and appears to consist of a single polypeptide chain.

804 citations

Journal ArticleDOI
01 Nov 2001-Blood
TL;DR: Understanding the complex interaction between different cellular programs provides insights into sensitivity or resistance of tumor cells and identifies molecular targets for rational therapeutic intervention strategies.

799 citations

Journal ArticleDOI
TL;DR: The respective results show that the plasminogen activators in urine and cell culture media are generally of lower molecular weight than those in plasma, and that proteases bound to α2-macroglobulin recover the ability to attack macromolecular substrates after exposure to sodium dodecyl sulfate while retaining the electrophoretic mobility of the protease inhibitor complex.
Abstract: We have (a) screened a variety of cell lines and body fluids for plasminogen activators and (b) studied the activity of proteases bound to alpha2- macroglobulin after exposing the complexes to partial degradation and/or denaturing procedures to unmask proteolytic activity. The respective results show (a) that the plasminogen activators in urine and cell culture media are generally of lower molecular weight than those in plasma; and (b) that proteases bound to alpha2-macroglobulin recover the ability to attack macromolecular substrates after exposure to sodium dodecyl sulfate while retaining the electrophoretic mobility of the protease inhibitor complex. This indicates that the protease and inhibitor are probably linked by covalent bonds. In contrast, other complexes formed between proteases and inhibitors of lower molecular weight (such as soybean or Kunitz inhibitors) are fully dissociated by sodium dodecyl sulfate (SDS). The experiments described were based on a new procedure for detecting proteolytic enzyme activity in SDS-polyacrylamide gels. The method relies on solutions of nonionic detergents for extracting SDS, after which the electrophoretic gel is applied to an indicator gel consisting of a fibrin- agar mixture. The method is sensitive, permitting the detection of proteinases in less than 1 mul of fresh plasma, and it is effective for resolving small differences in molecular weight. The procedure can be quantitated and, with minor modifications appropriate to each particular system, it has been applied to a broad spectrum of serine enzymes and proenzymes, including some that function in the pathways of fibrinolysis, coagulation and kinin-generation. Other potential applications appear likely.

791 citations

Journal ArticleDOI
TL;DR: This introductory article will focus on discussion of the essential roles of proteases in cell behavior and survival and death of all organisms, and the large collection of findings demonstrating their relevance in the control of multiple biological processes in all living organisms.

780 citations

Journal ArticleDOI
01 May 1998-Stroke
TL;DR: Matrix metalloproteinases (MMPs) are a family of proteolytic enzymes that degrade the extracellular matrix and are implicated in numerous pathological conditions including at...
Abstract: Background and Purpose—Matrix metalloproteinases (MMPs) are a family of proteolytic enzymes that degrade the extracellular matrix and are implicated in numerous pathological conditions including at...

767 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202350
2022113
2021358
2020434
2019358
2018472