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)

Chick embryo skin fibroblasts release transforming growth factor beta 1 that is able to modulate glycosaminoglycan synthesis and secretion. When incubated with individual classes of glycosaminoglycans, the factor's modulatory activity was altered. To determine whether direct interactions between transforming growth factor beta 1 and glycosaminoglycans occur, we have assessed the activity of the growth factor after pre-incubation with single classes of glycosaminoglycans by assaying its inhibitory effect upon the proliferative response of thymocytes stimulated with interleukin-1. Untreated transforming growth factor beta 1 suppressed the proliferative response of thymocytes to interleukin-1, as did transforming growth factor beta 1 pre-incubated with sulphated glycosaminoglycans. By contrast, transforming growth factor beta 1 lost its inhibitory capacity when preincubated with high molecular weight hyaluronic acid. Digestion of transforming growth factor beta 1-hyaluronic acid complex with hyaluronidase released active transforming growth factor beta 1. Trypsin degraded transforming growth factor beta 1 alone, but did not degrade the transforming growth factor beta 1-hyaluronic acid complex. These results suggest that hyaluronic acid interacts with transforming growth factor beta 1, thus protecting the factor from tryptic degradation and may be a means of concentrating growth factor activity.
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PMID:Transforming growth factor beta 1-hyaluronic acid interaction. 764 25

Bovine articular cartilage and synovial fluid (SF) were co-incubated with one of three enzymes selected to destroy each of the three major contenders for the active ingredient imparting such remarkable load-bearing lubrication to the normal joint. Destroying hyaluronic acid (HA), alias hyaluronan, with hyaluronidase, both frictional and wear tests displayed no significant change in accordance with most previous studies of SF alone. Destroying surface-active phospholipid (SAPL) with phospholipase A2, there was a highly significant dose-dependent compromise of lubrication as recorded on both tests. Trypsin produced a somewhat surprising result in that lubrication of the cartilage actually improved. This result can be interpreted as indicating that lubricin is not the lubricant per se, but, as a water-soluble, macromolecular, proteinaceous carrier for phospholipid, its destruction caused more SAPL to be deposited as the true load-bearing lubricant. These results are discussed in the context that SAPL, lubricin and HA each have specific roles in a comprehensive lubrication system.
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PMID:Enzymatic identification of the load-bearing boundary lubricant in the joint. 956 67

A lectin was isolated from the venom of scorpion Buthus occitanus sp. by means of Sephadex G-50 gel filtration and CM-cellulose ion exchange chromatography. The homogeneous lectin preparation consisted of homodimeric molecules with a subunit Mr of 9.3 kDa. Glycine, alanine, and serine dominated in the lectin amino acid composition. The lectin was a glycoprotein containing 20% carbohydrates (predominantly mannose and glucose). Trypsin-treated murine erythrocytes agglutinated at the lectin concentration of 32 micrograms/ml. Hemagglutination was inhibited by carbohydrates (L-fucose > D-glucose > L-rhamnose > D-xylose). The lectin revealed no phospholipase or hyaluronidase, nor toxic activity.
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PMID:[Isolation and some properties of a lectin from the venom of the Vietnamese scorpion Buthus occitanus sp]. 1160 80

The high molecular weight arylamidase-alkaline phosphatase-complex from rat kidney microsomes [1] was carefully dissociated by means of treatment with several hydrolytic enzymes or by acidification. Trypsin, chymotrypsin and pronase cause a selective solubilization of the enzymes discernible at their different electrophoretic mobility in polyacrylamide gel. The lower migrating zone represents phosphatase, the faster migrating zone shows arylamidase activity (molecular weights 180,000 and 172,000, respectively). Incubation of the complex with papain, lipase, neuraminidase or hyaluronidase and incubation at acid conditions (pH optimum 5.0) in the absence of any enzyme also yields in the appearance of two protein bands. In contrast to the alkaline hydrolases the acid hydrolases, the pH 5-treatment and with a certain degree also the lipase liberate a second arylamidase zone lying in the phosphatese containing zone during polyacrylamide gel electrophoresis. Treatment with SDS and subsequent SDS-polyacrylamide gel electrophoresis also results in a dissociation of the complex, but only in one protein fragement (approx, molecular weight 205,000).
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PMID:??? 1194 35


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