Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.6.4 (chondroitinase)
 2,039 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Thirty-nine strains of gram-positive microaerophilic cocci isolated from cases of heifer and dry-cow mastitis were biochemically characterized with the API 50E and API-ZYM test kit systems, gas-liquid chromatography for analysis of end products of glucose metabolism, and anaerobic biochemical tests (L. V. Holdeman, E. P. Cato, and W. E. C. Moore, Anaerobe Laboratory Manual, Virginia Polytechnic Institute, Blacksburg, 1977). Strains were screened for production of a variety of extracellular enzymes on substrate-containing agar plates and for hemolysin and coagulase production. Antibiotic susceptibility and sensitivity tests were also performed. The microaerophilic cocci displayed homogeneity with respect to the majority of the biochemical tests used; i.e., greater than or equal to 90% of the strains were consistently positive or negative in any one test and probably represent one species. All produced deoxyribonuclease, ribonuclease, and hyaluronidase, and 92% were positive for chondroitin sulfatase. Catalase and coagulase tests were negative. Greening was observed on bovine blood agar. Acetic and succinic acids were produced by all strains as the only detectable products of glucose metabolism. The strains were susceptible to penicillin G, cefoxitin, doxycycline, and chloramphenicol and were resistant to clindamycin, novobiocin, and metronidazole. Their taxonomic position remains unclear.
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PMID:Biochemical characterization of unidentified microaerophilic cocci isolated from heifer and dry-cow mastitis. 39 19

The bone inducing factor derived from BF osteosarcoma was purified in the following manner. Step 1. The sarcoma, grown in CBA mice, was excised and lyophilized. Step 2. The powder was washed with chilled acetone. Step 3. The acetone-treated powder was then homogenized with chilled distilled water. Step 4. Washing with 0.15M KCl. Step 5. The precipitate was incubated in in 0.2 N NH2OH, pH7.0, for 48 H at 25 degrees. After Step 5, the bone-forming activity showed a slight increase; however, the factor remained insoluble. The properties of the factor were as follows. The factor is relatively relatively heat stable; the osteogenic activity survived the treatment at 75 degrees for 15 min or at 55 degrees for 19 h. The activity was easily lost by mechanical shaking. Incubation with DNase, RNase, neuraminidase, chondroitinase ABC and beta-galactosidase left the osteogenic activity intact, but treatment with either pronase or collagnease destroyed this activity. The results suggest that the factor may be a protein. The activity was seen with the lyophilized BF osteosarcoma cells (without matrix), and it is probable that the factor was exclusively synthesized in the cells. The bone formation, observed across a millipore filter when living BF osteosarcoma enclosed in a millipore chamber was implanted in mice, suggests the synthesis and secretion of the factor from the cells.
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PMID:Studies on a factor responsible for new bone formation from osteosarcoma in mice. 105 58

We have isolated a factor that copurifies with chondroitin sulfate proteoglycan secreted by mouse splenocytes and some murine T-cell hybridomas. This factor will stimulate proliferation and plaque-forming cell differentiation of B lymphocytes from mouse spleens, even after T cells have been depleted (less than 2% Thy 1.2-bearing cells). Adherent macrophages enhance the activity of this factor, but their function can be replaced in macrophage- and T-cell-depleted populations by small concentrations of a protein mitogen from Salmonella typhimurium. The stimulatory fraction contains chondroitin sulfate, a major protein which has a molecular weight of 74,000 and a minor moiety at 50,000. Stimulatory activity of this material is destroyed by (i) boiling, (ii) mild alkali treatment, and (iii) protease digestion. It is unaffected by RNase and chondroitinase treatments, suggesting that the factor is a protein. Our data define a new B-cell stimulatory substance(s) and suggest that it may be associated with chondroitin sulfate proteoglycan secreted by immune cells.
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PMID:Stimulation of mouse B cells by a factor that coisolates with T-cell proteoglycan. 309 Dec 76

Rat brain extracts contain two heat-stable, nondialyzable inhibitors of tubulinyl-tyrosine carboxypeptidase. One of the inhibitors was sensitive to ribonuclease and insensitive to trypsin and pronase, indicating that the inhibitor is RNA. This is supported by the observation that purified RNA from rat brain inhibited the enzyme activity to the same extent as similar amounts of the endogenous RNA. Similar results were obtained with calf liver RNA. The other inhibitor was purified by chromatography on a DEAE-Sephadex and identified as proteoglycan. The elimination of the protein moiety of the proteoglycan resulted in a small increase of its inhibitory activity. Glycosaminoglycan was released from the proteoglycan by beta elimination, indicating that the linkage between glycosaminoglycan and the protein moiety is through an O-glycosidic bond. The glycosaminoglycan contains uronic acid, hexosamine and sulfate in a molar ratio of 1:1.01:0.99, respectively. Treatment of the glycosaminoglycan with chondroitinase ABC completely abolished its inhibitory activity. Chondroitin sulfate A, chondroitin sulfate B, chondroitin sulfate C, and the brain glycosaminoglycan inhibited tubulinyl-tyrosine carboxypeptidase to the same extent when used in comparable amounts.
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PMID:Inhibition of tubulinyl-tyrosine carboxypeptidase by brain soluble RNA and proteoglycan. 616 Nov 29

All strains of Legionella pneumophila tested produced detectable levels of extracellular protease, phosphatase, lipase, deoxyribonuclease, ribonuclease, and beta-lactamase activity. Weak starch hydrolysis was also demonstrated for all strains. Elastase, collagenase, phospholipase C, hyaluronidase, chondroitinase, neuraminidase, or coagulase were not detected in any of these laboratory-maintained strains.
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PMID:Extracellular enzymes of Legionella pneumophila. 626 49