Results 251 to 260 of about 278,197 (298)
Proteolysis in the rat lung: hypoxia and evidence for an inhibitor of proteolysis
American Journal of Physiology-Endocrinology and Metabolism, 1981 We labeled proteins with [14C]phenylalanine in rats breathing air and assessed the rate of proteolysis in the isolated ventilated lung by measuring the accumulation of [14C]phenylalanine in the medium perfusing the lung. Ventilation with 0% O2 decreased the rate of proteolysis and the ATP content in the lung 60%.
M J, Chiang +3 more
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Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways
New Phytologist, 2017 Proteases can either digest target proteins or perform the so-called 'limited proteolysis' by cleaving polypeptide chains at specific site(s). Autophagy and the ubiquitin-proteasome system (UPS) are two main mechanisms carrying out digestive proteolysis.
Panagiotis N. Moschou +2 more
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Current Opinion in Clinical Nutrition and Metabolic Care, 2001
The mechanisms of proteolysis remain to be fully defined. This review focuses on recent advances in our understanding of the ubiquitin-proteasome-dependent pathway, which is involved in the control of many major biological functions. The ubiquitinylation/deubiquitinylation system is a complex machinery responsible for the specific tagging and proof ...
Attaix, Didier +3 more
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The mechanisms of proteolysis remain to be fully defined. This review focuses on recent advances in our understanding of the ubiquitin-proteasome-dependent pathway, which is involved in the control of many major biological functions. The ubiquitinylation/deubiquitinylation system is a complex machinery responsible for the specific tagging and proof ...
Attaix, Didier +3 more
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1977
The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS
R, Mecham, J A, Foster, C, Franzblau
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The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS
R, Mecham, J A, Foster, C, Franzblau
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Trends in Genetics, 1999
Our present understanding of intracellular protein degradation developed from an attempt to understand the metabolic stability of proteins in cells. With the unravelling of its complex biochemical machinery has come a realization that protein degradation plays an important role in the most crucial events in the cell cycle, in signal transduction and in
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Our present understanding of intracellular protein degradation developed from an attempt to understand the metabolic stability of proteins in cells. With the unravelling of its complex biochemical machinery has come a realization that protein degradation plays an important role in the most crucial events in the cell cycle, in signal transduction and in
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Proteolysis as a Regulatory Mechanism
Annual Review of Genetics, 2004▪ Abstract  Proteases can play key roles in regulation by controlling the levels of critical components of, for example, signal transduction pathways. Proteolytic processing can remove regulatory proteins when they are not needed, while transforming others from the dormant into the biologically active state.
Ehrmann, Michael, Clausen, Tim
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Intramembrane proteolysis by presenilins
Nature Reviews Molecular Cell Biology, 2000Many neurodegenerative diseases involve the deposition of insoluble amyloid molecules. In Alzheimer's disease, for example, the amyloid beta-peptide (A beta) is the main component of the characteristic senile plaques. Proteolytic enzymes called secretases are involved in generating A beta, and one of these may have been identified as presenilin--a ...
H, Steiner, C, Haass
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The course of proteolysis of lysozyme
Archives of Biochemistry and Biophysics, 1956Abstract The course of proteolysis of lysozyme by chymotrypsin, trypsin, papain at three pH's, and pepsin is reported with tabulation of progressive exposure of 15 N-residue types and 12 C-residue types. A marked similarity in pattern of hydrolysis has been observed.
S W, FOX, T L, HURST
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Biochemical and Biophysical Research Communications, 1989
The calpain-induced proteolysis of tau associated with twice-cycled microtubules or from a total brain heat-stable fraction was studied. Twice-cycled microtubule tau was rapidly hydrolyzed by calpain. In contrast, tau purified from the total brain heat-stable fraction was very resistant to degradation by calpain.
G V, Johnson, R S, Jope, L I, Binder
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The calpain-induced proteolysis of tau associated with twice-cycled microtubules or from a total brain heat-stable fraction was studied. Twice-cycled microtubule tau was rapidly hydrolyzed by calpain. In contrast, tau purified from the total brain heat-stable fraction was very resistant to degradation by calpain.
G V, Johnson, R S, Jope, L I, Binder
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Proteolysis of Bovine Immunoglobulins
International Archives of Allergy and Applied Immunology, 2009Bovine serum IgG1, colostral IgG1 and serum IgG2 with anti-ferritin activity were digested with pepsin or trypsin. Their fragments were characterized by immunoelectrophoresis, gel electrophoresis and gel filtration; their ferritin-binding ability was determined.
O, de Rham, H, Isliker
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