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PMID: 6781490 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Proteinase activity in chondroitin lyase (chondroitinase) and endo-beta-D-galactosidase (keratanase) preparations and a method to abolish their proteolytic effect on proteoglycan.

The Biochemical journal ·Vol. 191 ·No. 1 ·1980-10-01 ·Pages 203-7

Oike Y, Kimata K, Shinomura T, Suzuki S

Abstract

Significant amounts of proteinase activity have been found in chondroitin ABC lyase (EC 4.2.2.4), chondroitin AC II lyase and endo-beta-D-galactosidase (keratanase) from commercial sources. It would appear, therefore, that certain earlier biochemical and histochemical studies, which employed these commercial enzyme preparations for their presumed ability to degrade only glycosaminoglycans, may require re-evaluation. A mixture of EDTA, N-ethylmaleimide, phenylmethanesulphonyl fluoride and pepstatin abolishes the effect of the contaminating proteinases on proteoglycan with less significant effect on the chondroitin lyase or keratanase activity.

MeSH Terms

Animals Chick Embryo Chondroitin Lyases/isolation & purification Chondroitinases and Chondroitin Lyases/isolation & purification Chromatography, Gel Drug Contamination Endopeptidases Galactosidases/isolation & purification Methods Pepstatins Proteoglycans beta-Galactosidase/isolation & purification

Chemicals

Pepstatins Proteoglycans Galactosidases beta-Galactosidase Endopeptidases Chondroitin Lyases Chondroitinases and Chondroitin Lyases

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Oike Y

Kimata K

Shinomura T

Suzuki S

References (10)

10 references, click to expand

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Effect of pepstatin on acid proteases.
J Antibiot (Tokyo). 1971 Oct;24(10):687-94 PMID: 4945810
Sequential degradation of keratan sulfate by bacterial enzymes and purification of a sulfatase in the enzymatic system.
J Biol Chem. 1975 Feb 10;250(3):905-11 PMID: 1112796
Purification of Keratan Sulfate-endogalactosidase and its action on keratan sulfates of different origin.
J Biol Chem. 1975 Feb 10;250(3):912-7 PMID: 234443
Crystallization and some properties of chondroitinase from Arthrobacter aurescens.
J Biol Chem. 1975 Mar 10;250(5):1824-8 PMID: 234466
Action of chondroitinases. I. The mode of action of two chondroitinase-AC preparations of different origin.
J Biochem. 1976 Dec;80(6):1201-7 PMID: 138676
Role of hyaluronic acid in the in vivo aggregation of cartilage proteoglycans.
Connect Tissue Res. 1978;5(4):237-48 PMID: 150964
The occurrence of low buoyant density proteoglycans in embryonic chick cartilage.
Biochem Biophys Res Commun. 1978 Dec 29;85(4):1431-9 PMID: 570400
Structural analysis of chick-embryo cartilage proteoglycan by selective degradation with chondroitin lyases (chondroitinases) and endo-beta-D-galactosidase (keratanase).
Biochem J. 1980 Oct 1;191(1):193-207 PMID: 6781489
A submicrodetermination of glucose.
J Biol Chem. 1949 Nov;181(1):149-51 PMID: 15390401

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1910203

Published

1980-10-01

Pages

203-7

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1162198

Subset

External Links

PubMed source DOI: 10.1042/bj1910203 PMC Full Text View journal details

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Proteinase activity in chondroitin lyase (chondroitinase) and endo-beta-D-galactosidase (keratanase) preparations and a method to abolish their proteolytic effect on proteoglycan.

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