The lanthanide-enhanced affinity chromatography of clostridial collagenase.

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Clostridiopeptidase A (EC 3.4.24.3) did not bind to a collagen affinity column in the absence of Ca2+, but did so in the presence of lanthanide ions (Ln3+). The sequestered enzyme could be eluted with EGTA. For the four Ln3+ ions tested, the order of efficiency in promoting enzyme binding, Sm3+ greater than Lu3+ greater than Er3+ much greater than La3+, reflected their relative abilities to inhibit clostridiopeptidase A. By using Sm3+ as an adjunct, it proved possible to separate a highly active preparation of collagenase from crude clostridial collagenase. Sodium dodecyl sulphate/polyacrylamide-gel-electrophoretic analysis of the preparation revealed a major protein of Mr 95000 and a minor component of Mr 82000. As both were stained by periodic acid/Schiff reagent, they were probably glycoproteins.

Original languageEnglish (US)
Pages (from-to)553-556
Number of pages4
JournalBiochemical Journal
Volume225
Issue number2
StatePublished - Jan 15 1985
Externally publishedYes

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Microbial Collagenase
Affinity chromatography
Lanthanoid Series Elements
Collagenases
Affinity Chromatography
Ions
Periodic Acid
Egtazic Acid
Enzymes
Sodium Dodecyl Sulfate
Glycoproteins
Collagen
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

The lanthanide-enhanced affinity chromatography of clostridial collagenase. / Evans, Christopher H.

In: Biochemical Journal, Vol. 225, No. 2, 15.01.1985, p. 553-556.

Research output: Contribution to journalArticle

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