| Literature DB >> 239695 |
Abstract
Inorganic pyrophosphatase (pyrophosphate phosphohydrolase; EC 3.6.1.1) was purified from pig scapula cartilage by fractionation with N-cetylpyridinium chloride and (NH4)2SO4, followed by ion-exchange and gel-filtration chromatography. Enzyme preparations of high purity were obtained, with specific activities (100-400 units/mg) higher than those previously described for mammalian pyrophosphatases. The enzyme activity could be separated into several subfractions on ion-exchange columns.Entities:
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Year: 1975 PMID: 239695 PMCID: PMC1165379 DOI: 10.1042/bj1470103
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857