Author:
Sen Mira,Drance S. M.,Woodford V. R.
Abstract
Two components of carbonic anhydrase have been separated in partially purified forms from the soluble proteins of bovine lens. During the chromatographic separation on diethylaminoethyl cellulose columns, the total carbonic anhydrase increased, on an average, by nine times. The implications of these findings are that bovine lens carbonic anhydrase may exist in the form of two isoenzymes and that there may be a naturally occurring in vivo inhibitory mechanism regulating the activity of bovine lens carbonic anhydrase in situ.
Publisher
Canadian Science Publishing
Cited by
7 articles.
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