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PMID: 207263 Published · ppublish English Journal Article

Neutral metallo-proteinases of rabbit bone. Separation in latent forms of distinct enzymes that when activated degrade collagen, gelatin and proteoglycans.

The Biochemical journal ·Vol. 171 ·No. 2 ·1978-05-01 ·Pages 493-6

Sellers A, Reynolds JJ, Meikle MC

Abstract

Rabbit bones in culture produce specific collagenase and neutral metallo-proteinase activity in latent forms that can be activated by either 4-aminophenylmercuric acetate or trypsin. Latent neutral metallo-proteinase activity was resolved by gel filtration into two enzymes, distinct from collagenase, that degrade gelatin and cartilage proteoglycans.

MeSH Terms
Animals Bone and Bones/enzymology Collagen/metabolism Endopeptidases/metabolism Enzyme Activation Gelatin/metabolism Metalloproteins/metabolism Microbial Collagenase/metabolism Organ Culture Techniques Proteoglycans/metabolism Rabbits
Chemicals
Metalloproteins Proteoglycans Gelatin Collagen Endopeptidases Microbial Collagenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Sellers A
Reynolds J J
Meikle M C
References (11)
11 references, click to expand
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    J Clin Invest. 1976 Oct;58(4):1030-41 PMID: 9425
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    Biochem J. 1974 May;139(2):359-68 PMID: 4374931
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    Biochem J. 1977 Dec 1;167(3):775-85 PMID: 23763
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1978-05-01
Pages
493-6
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1183981
Subset
IM
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