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PMID: 164924 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Studies on the interaction between heparin and mouse bone collagenase.

Biochimica et biophysica acta ·Vol. 385 ·No. 1 ·1975-03-14 ·Pages 41-50

Sakamoto S, Sakamoto M, Goldhaber P, Glimcher MJ

Abstract

Mouse bone collagenase was found to be tightly bound to a heparin-substituted gel at low ionic strength. The bond was reversible, however, and the collagenase could be elutted at high ionic strength. In addition to providing a method for purifying the enzyme with high yield, the results suggest that the strong ionic bond between heparin and collagenase may partially explain the mechanism wherein heparin enhances the activity of mouse bone collagenase.

MeSH Terms
Animals Bone and Bones/enzymology Chromatography, Affinity Heparin/pharmacology Mice Microbial Collagenase/isolation & purification,metabolism Molecular Weight Osmolar Concentration Protein Binding Sepharose Tibia/enzymology
Chemicals
Heparin Sepharose Microbial Collagenase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sakamoto S
Sakamoto M
Goldhaber P
Glimcher M J
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1975-03-14
Pages
41-50
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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