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)

Adult rabbit zonular fibers maintained in their native condition were treated with collagenase, alpha-chymotrypsin and hyaluronidase, and were observed with the electron microscope. The results obtained were as follows: 1. Collagenase digested the lens capsule, but not the zonular fibers. 2. Long time collagenase action obscured the cell membrane of the lens epithelium and the basal lamina of the ciliary epithelium. 3. Washing with 0.9% NaCl increased the collagenase action on the lens capsule. 4. Alpha-chymotrypsin digested the zonular fibers and the zonular lemalla, but not the lens capsule and the basal lamina of the ciliary epithelium. 5, Hyaluronidase only slightly changed the lens capsule. 6. The vitreous fibers were digested by collagenase, but not by alpha-chymotrypsin or hyaluronidase. Thes results together with the review of recent literature indicate that the zonular fiber has a nature close to that of the microfibril of elastic fiber.
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PMID:Electron microscopic studies on zonular fibers. II. Changes of the zonular fibers after the treatment with collagenase, alpha-chymotrypsin and hyaluronidase. 16 41

Cerebral neurons in monolayer cultures, subjected to 25 micrograms/ml trypsin, lose after 10 min about 43.5% and 40.5% of the ability to bind 125I-labeled tetanotoxin as measured at 0-4 degrees C and 37 degrees C respectively. These losses are maximal by 30 min and can be prevented by 1.5 mg/ml soybean trypsin inhibitor. Chymotrypsin but not collagenase or hyaluronidase is also effective in reducing binding of toxin to cells. The trypsin-insensitive toxin-binding activity can be further eliminated by treatment with sialidase or by cell extraction with methanol. Fixation of cells with 3.5% paraformaldehyde or 2% glutaraldehyde also results in a marked decrease of 52.4% and 25% respectively in the toxin-cell association. Methanol or sialidase but not trypsin removes the remaining binding activity. About one-third of the lipid-linked and protein-linked sialic acid is removed after sialidase treatment whereas 1% and 9.4% respectively are removed after trypsin treatment. The data are consistent with the possibility that, in addition to a sialic acid component, binding of tetanotoxin to nerve cells is facilitated by a trypsin-removable and formaldehyde-inactivated component. There was no evidence for a polypeptide to substitute gangliosides as receptors for tetanotoxin. On the contrary, solubility in organic solvents and interaction of the extracted products with labeled toxin remain the major proof that gangliosides are the putative receptors for tetanotoxin.
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PMID:Tetanus toxin receptors on nerve cells contain a trypsin-sensitive component. 394 36

Vitreous from bovine, human and chick embryo has been found to contain a trypsin inhibitory activity. Chymotrypsin-inhibitory activity was also identified in bovine and chick embryo vitreous. Following either ultrafiltration or Bio Gel P-10 chromatography, these activities appear in fractions having a molecular weight greater than 10000 MW (ultrafiltration) or greater than 13000 MW (P-10 void volume), and are separable from low molecular weight aortic endothelial cell growth inhibitory activity present either in the ultrafiltrate or P-10 retarded volume. Treatment of the trypsin inhibitory fraction with hyaluronidase had no effect on trypsin inhibition, nor did addition of hyaluronic acid inhibit trypsin. Chick embryo vitreous and hyalocyte-conditioned medium were found to contain aortic endothelial cell growth inhibitory activity in both the void volume and retarded volume fractions following Bio Gel P-10 chromatography. Both the 6200 MW bovine vitreous endothelial cell growth inhibitor and the high molecular weight chick embryo vitreous endothelial cell growth inhibitor (greater than 13000 MW) were similar, in that most of the activity did not bind to heparin linked to Sepharose CL-6B.
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PMID:Inhibition of vascular endothelial cell growth and trypsin activity by vitreous. 409 50