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. 1975 Mar 28;386(1):80-6.
doi: 10.1016/0005-2795(75)90248-2.

Application of affinity chromatography to the purification of collagenase for the isolation of insoluble elastin

A Serafini-Fracassini, J M Field, G W Rodger, M Spina

Application of affinity chromatography to the purification of collagenase for the isolation of insoluble elastin

A Serafini-Fracassini et al. Biochim Biophys Acta. .

Abstract

ClostrIdium histolyticum collagenase (clostridiopeptidase A, EC 3.4.4.19) was purified by batchwise separation with DEAE-cellulose followed by affinity chromatography on a column of alkali-treated elastin. The N-terminal amino acid profile of elastin isolated from bovine ligamentum nuchae using this enzyme preparation was compared with that of a duplicate sample purified with a mixture of collagenase I and II (Yoshida, E, and Noda, H. (1965) Biochim. Biopsys. Acta 105, 562-574). An approx. three-fold decrease in the molar concentration of N-terminal residues and a considerable reduction in their number was obtained by using the former enzyme preparation.

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