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

The lysosomal glycosidase activity of the eye tissues (the sclera and cornea), the bone tissues and cartilage were studied. The intraperitoneal injection of tyrocalcitonine (TCT), deoxycorticosterone (DOCS), hydrocortisone (HC), and somatotropic hormone (STH) influenced both the activity of beta-galactosidase, beta-glucosidase, and hyaluronidase, the the functional state of thy lysosomal membranes of the connective tissues under investigation. GC and STH caused stabilization, whereas DOCS and large doses of TCT--a labilizing effect on the lysosomal membranes and tissues understudy. The absolute activity of the enzymes in the homogenates decreased after the HC and STH injection. DOCS produced an opposite effect.
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PMID:[Responses of different types of connective tissue to hormone administration]. 89 Jan 33

1. In human plasma, an enzyme is present which hydrolyzes 4-methylumbelliferyl-tetra-N-acetylchitotetraoside. The function of this enzyme is unknown. 2. We have examined whether hyaluronidase, neutral endoglucosaminidase, N-acetyl-beta-D-hexosaminidase, aspartylglucosaminidase, beta-D-glucosidase, and chitobiase could hydrolyze MU-TACT. The results obtained are detailed below. 3. A purified commercial preparation of hyaluronidase does not hydrolyze MU-TACT. 4. Substrate specificity requirements, pH optimum and subcellular localization indicate that neutral endoglucosaminidase is distinguishable from MU-TACT hydrolase. Also commercial neutral endoglucosaminidase D and H have no affinity towards MU-TACT. 5. N-Acetyl-beta-D-hexosaminidase is different from MU-TACT hydrolase for the following reasons: (a) a purified enzyme preparation does not hydrolyze MU-TACT; (b) there is no correlation in the activity of the enzymes; (c) MU-TACT hydrolase is not deficient in cells of a patient with a deficiency of total N-acetyl-beta-D-glucosaminidase; and (d) the 2 enzymes have very different chromatographic characteristics and Con A binding properties. 6. Enzyme characteristics, substrate structural requirements and a lack of correlation with MU-TACT hydrolase activity suggest that aspartylglucosaminidase, beta-D-glucosidase, and chitobiase are not involved in the hydrolysis of MU-TACT. 7. None of the enzymes which we have considered corresponds to MU-TACT hydrolase. The exact nature and the function of the enzyme remains an enigma.
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PMID:Evaluation on the hydrolysis of methylumbelliferyl-tetra-N-acetylchitotetraoside by various glucosidases. A comparative study. 843 79