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Science 13 November 1964:
Vol. 146. no. 3646, pp. 942 - 944
DOI: 10.1126/science.146.3646.942
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Articles

Collagenolytic Activity of Intact and Necrotic Connective Tissue

E. R. Goldstein 1, Y. M. Patel 1, and J. C. Houck 1

1 Biochemical Research Laboratory, Children's Hospital, Washington, D.C. 20009, and Department of Biochemistry, Georgetown University Medical and Dental School, Washington, D.C. 20007

Isotonic saline extracts of both intact and necrotic skin of the rat were capable of releasing over 50 percent of the hydroxyproline content of soluble collagen as dialyzable, peptide-bound amino acid only after prior, limited proteolytic activation of trypsin. These "activated" extracts could also solubilize insoluble collagen to release dialyzable hydroxyproline containing peptides. This collagenolytic activity was maximal at pH 5.5 and was not inhibited by soybean trypsin inhibitor, ethyl-enediaminetetraacetic acid, or heavy metal salt. The "activated" extracts showed no general proteolytic activity toward denatured hemoglobin. The collagenolytic activity was destroyed both by heat and by extensive tryptic proteolysis.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Induction of Collagenolytic and Proteolytic Activities in Rat and Human Fibroblasts by Anti-Inflammatory Drugs.
J. C. Houck and V. K. Sharma (1968)
Science 161, 1361-1362
   Abstract »    PDF »
Hydroxyproline and Collagen Metabolism: Clinical Implications * Combined Clinical Staff Conference at the National Institutes of Health.
A. SJOERDSMA, S. UDENFRIEND, H. KEISER, and E. C. LEROY (1965)
Ann Intern Med 63, 672-694
   Abstract »    PDF »


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