Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A novel collagen chain, termed alpha C, has been isolated from human placenta by limited pepsin digestion. The collagen containing the alpha C chain copurifies with placental AB collagen during selective salt precipitation but is virtually absent from fetal birth membranes, which contain relatively larger amounts of AB. Both native AB and alpha C-containing collagens are resistant to human skin collagenase under conditions that support cleavage of type I by greater than 90%. The alpha C chain was separated from alpha B by phosphocellulose chromatography and subsequently from alpha P by chromatography on CM-cellulose. Its amino acid composition is distinct from alpha A and alha B although all three chains posses compositional features in common; the carbohydrate content of the alpha C chain was intermediate between those of alpha A and alpha B. Analysis by NaDodSO4-polyacrylamide gel electrophoresis of peptides produced by CNBr cleavage and by limited digestion with the enzyme mast cell protease indicated different and unique products for the alpha A, alpha B, and alpha C chains. The data support the existence of another collagen chain which is related to the alpha A and alpha B chains but which is structurally unique. The proteins containing these chains may in turn comprise a subfamily of collagen isotypes which represents a divergence from and/or specialization of the type IV basement membrane collagens.
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PMID:Characterization of a novel collagen chain in human placenta and its relation to AB collagen. 22 19

We measured the relative solubility of collagen in acetic acid after pepsin digestion and tentatively identified the types of collagen present in corneas of rabbits of various ages and in corneal scar tissue, using hydroxyproline assays and polyacrylamide gel electrophoretic analyses. More than 80% of the collagen in normal developing rabbit cornea was soluble after pepsin treatment; no more than 45% of that in two-week-old corneal scars was soluble. The predominant collagens in normal cornea and healing tissue were types I and AB. Type AB increased from 6% of the total collagen in fetal cornea to 11% in cornea from young adults. Collagen from two-week-old corneal wounds contained 16% type AB. Corneal type AB collagen was less soluble and more resistant to degradation by mammalian collagenase than was type I collagen. Unlike the normal cornea, in healing tissue the relative rate of synthesis of type I to type AB collagens did not correspond to their deposition. These results suggest a basic alteration in the molecular structure of the corneal scar, which may be instrumental in preventing the healing tissue from producing a normal, functioning organ.
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PMID:Quantitative analysis of collagen from normal developing corneas and corneal scars. 729 90