Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

KCl extract from rat kidney, rat liver, and Morris hepatomas inhibited [3H]thymidine incorporation into cultured cells. Tissues came from male inbred BUF rats. The most pronounced inhibition was achieved with the kidney extract. Protein synthesis was not inhibited during a 24-hour exposure of the cells to the inhibitor. Incorporation of [3H]deoxycytidine was inhibited, as was cell growth, when the kidney KCl extract was present for several days. [3H]thymidine incorporation was inhibited almost immediately after the addition of the extract. The inhibition was reversible. Regular [3H]thymidine incorporation was restored 24 hours after removal of the inhibitor, which was neither arginase nor a thymidine-degrading enzyme. The inhibitor was stable to heat (80 degrees C for 10 min) and resistant to trypsin, pronase, DNase, and RNase. Exposure of the extract to proteolytic enzymes, hyaluronidase, and neuraminidase resulted in a loss of inhibitory activity only after extensive dialysis of the treated extract. The inhibitor appeared to be a mucoprotein in which the carbohydrate moiety may be responsible for the inhibition. The KCl extract also inhibited RNA synthesis and DNA synthesis by the de novo pathway. The inhibition of phosphorylation of thymidine, however, appeared to be the primary action of the inhibitor.
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PMID:Inhibition of tritiated thymidine incorporation in cultured cells by rat kidney extract. 15 53

Isolated cardiac muscle cells enzymatically digested with collagenase and hyaluronidase from whole rat myocardium demonstrate the characteristics of an intact membrane in that they tolerate millimolar concentrations of free Ca2+ and exhibit phasic contractions with electrical excitation. These isolated cells maintain their characteristic A-I band striation patterns when at rest or during contraction. An apparatus has been developed to directly image these cells with phase-contrast micrography onto a 1,728-element charge-coupled device photodiode array for rapid data storage in a digital computer. The digitized striation pattern profile was analyzed for individual and average sarcomere spacing. In isotonic media the average resting sarcomere length ranged from 1.77 to 1.91 micrometers in 13 cells, with a mean length of 1.83 +/- 0.12 micrometers. Electrically stimulated phasic contractions in three cells demonstrated a synchronous 20% decrease in sarcomere spacing to a mean of 1.51 micrometers. Striation spacing decreased under hypertonic stress but elongated only up to 1.93 micrometers in hypotonic solutions, suggesting that some internal elastic constraint exists that limits elongation of the cell.
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PMID:Direct measurement of sarcomere length from isolated cardiac cells. 627 4

Synovial fluid was found to contain an inhibitor of neutrophil chemotaxis. The activity of this inhibitor was masked in native synovial fluid, but could be detected in fluid in which complement had been deactivated by mild heating. The inhibitor was most effective against the chemotactic activity of zymosan-activated serum (C5ades arg). It had little effect when N-formyl-methionyl-leucyl-phenylalanine served as chemoattractant. Inhibition was not the result of a direct effect on the neutrophils, since incubation of cells with synovial fluid did not alter their chemotactic response. The inhibitory activity was destroyed by boiling the synovial fluid or treating it with trypsin, suggesting that it is a protein (or proteins); it was not affected by hyaluronidase treatment. Gel filtration revealed that the inhibitor was present in native as well as decomplemented synovial fluid, and that its molecular weight was in the vicinity of 25,000. It is proposed that this inhibitory activity plays a role in the regulation of the inflammatory response in joints.
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PMID:A chemotactic inhibitor in synovial fluid. 684 Aug 1

Members of the Streptococcus sanguis group (SSG) and Streptococcus milleri group (SMG) were screened for their ability to produce glycosidase, arylamidase (peptidase), protease, dextranase and glycosyltransferase activities. Species within each group produced unique patterns of activity. The most commonly produced glycosidases were beta-D-glucosidase, beta-D-galactosidase, N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase and the least commonly produced glycosidase activity was beta-fucosidase with Streptococcus intermedius (SMG) being the only species capable of producing the activity. For arylamidase activity, the most commonly produced type was lysine-arylamidase. Glycosidase and arylamidase activities were localized to particular sub-cellular fractions. alpha-galactosidase was found only in culture supernatant fluids whereas N-acetyl-beta-D-glucosaminidase was found in all fractions; the culture supernatant, cell wall, cell membrane and cytoplasm. No arylamidase activity was seen in culture supernatants. Phe-arg-arylamidase was found only in cytoplasmic fractions whereas val-pro-argarylamidase was found in cell walls, cell membranes and cytoplasmic fraction. Protease activity was measured as the degradation of bovine serum albumin (BSA) and casein. Casein was degraded by a number of strains whereas no species/strains were able to degrade BSA. Streptococcus intermedius, Streptococcus constellatus (SMG), Streptococcus mitior and Streptococcus defectivus (SSG) were the only species that produced hyaluronidase and no species produced chondroitin sulphatase. The groups were also examined for their abilities to produce glycosyltransferase and dextranase. Strep. sanguis, Streptococcus gordonii, Streptococcus mitis and Streptococcus oralis produced glucosyltransferase and, with the exception of the latter species, fructosyltransferase. No species within the SMG was capable of producing either glycosyltransferase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Degradative enzymes of oral streptococci. 778 31