Proteolysis of Tropoelastin
The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS gels with molecular weights of approximately 57,000, 45,000, 36,000, 25,000 and 13–14,000.
KeywordsCysteine Lysine Enzymatic Degradation Trypsin Fibril
Unable to display preview. Download preview PDF.
- 3.Foster, J.A., Mecham, R.P., and Franzblau, C, (1976) Biochem Biophys. Res. Comm., in press.Google Scholar
- 5.Mecham, R.P., Foster, J.A., Franzblau, C, (1976) Biochim. Biophys Acta, in press.Google Scholar
- 6.Mecham, R.P., Foster, J.A., Franzblau, C, (1976) in preparation.Google Scholar