Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Elastin was purified from baboon aorta using Achromobacter collagenase and its susceptibility to proteolysis by various enzymes was studied. Human leukocyte elastase (HLE) hydrolysed baboon aortic elastin 8 times faster than human cathepsin G. Bovine chymotrypsin had virtually no activity against this substrate. The kinetic constants V and [S50] of aortic elastin hydrolysis by HLE (0.15 microM) were 0.00286 mg x ml-1 x min-1 and 0.158 mg x ml-1, respectively. One mg of this elastin could be saturated with 5.6 micrograms of HLE. As with elastins isolated from other sources, the hydrolysis of baboon aortic elastin by HLE was highly sensitive to ionic strength, and a biphasic effect was obtained with increasing NaCl concentrations. A nearly 2-fold stimulation of elastolysis was observed at a 0.15M NaCl concentration. Further increase in ionic strength led to a continuous decrease of the rate of elastolysis which paralleled the decrease of adsorption of elastase to baboon aortic elastin. Cathepsin G, but not bovine alpha-chymotrypsin, was able to stimulate the rate of hydrolysis of baboon aortic elastin by HLE. A 1.7 fold stimulation was observed for a 1:1 molar ratio of the two proteinases and rose to 2.1 for a HLE/Cat. G ratio equal to 8.
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PMID:Susceptibility of baboon aorta elastin to proteolysis. 216 85

A new, sensitive assay based on the enzyme-linked immunosorbent assay has been developed for measuring elastolytic activity produced by invasive and/or metastatic tumor cells in culture. Elastin peptides, obtained by treating the insoluble protein with either oxalic acid, KOH, or chymotrypsin, are adsorbed onto the surface of cell culture microtiter plastic wells, and incubated with dilution of standard proteinases or viable normal or tumor cells. The total amount of immobilized elastin peptides is revealed by the mean of specific antibodies, and detected by a microplate reader, while dose- and time-dependent reduction of bound antibodies after incubation with proteases or cells is taken as a measure of elastin degradation. Adsorbed elastin has been found to be available as a substrate for purified enzymes, as well as for living melanoma cells (A2058 and B16-BL6), c-Ha-ras transformed rat embryo fibroblasts, and human pulmonary macrophages, as demonstrated by the release into the culture medium of lower molecular weight digestion products. No degradation was achieved by BALB/3T3 and rat embryo control fibroblasts, and no inhibition was produced by the presence of fetal calf serum which, on the contrary, potentiated the degradation by active cells. This new method, revealing degradation of only a few nanograms of soluble elastin peptides, can be used for studying the importance in tissue invasion and metastasis of elastolytic proteinases produced by cells in culture.
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PMID:Degradation of immobilized soluble elastin by tumor cells in culture: quantitation by ELISA. 239 16