Affinity chromatography of membrane fragments. Separation of carbonic anhydrase-enriched and -depleted brain membranes.
Chick brain membranes were fractionated by affinity chromatography on AH-Sepharose 6MB linked to p-sulfamylbenzoic acid, an inhibitor of carbonic anhydrase. Two major fractions were obtained. One, designated unbound fraction, representing 42% of the total membrane protein, eluted freely from the affinity adsorbent. A second fraction, designated specifically bound fraction, contained 36% of the total membrane proteins. In addition, 11% of the total membranes bound non-specifically and could be eluted only by the use of shearing forces. Various lines of evidence indicated that the sulfonamide binding site of membrane-bound carbonic anhydrase, in addition to the carbonic anhydrase inhibitor immobilized to AH-Sepharose 6MB, was responsible for the observed specific binding. The specifically bound fraction was highly enriched in carbonic anhydrase while the unbound fraction was completely devoid of this enzyme activity.[1]References
- Affinity chromatography of membrane fragments. Separation of carbonic anhydrase-enriched and -depleted brain membranes. Sharma, S.K., Babitch, J.A. J. Chromatogr. (1984) [Pubmed]
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