| Literature DB >> 6781490 |
Y Oike, K Kimata, T Shinomura, S Suzuki.
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.Entities:
Mesh:
Substances:
Year: 1980 PMID: 6781490 PMCID: PMC1162198 DOI: 10.1042/bj1910203
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857