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Comparative Study
. 1984 Jul;4(7):573-9.
doi: 10.1007/BF01121914.

Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification

R E Tashian, J T Johansen, E Christiansen, W R Chegwidden
Free article
Comparative Study

Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification

R E Tashian et al. Biosci Rep. 1984 Jul.
Free article

Abstract

Purified carbonic anhydrase isozymes I, II, and III (CA I, CA II, CA III) from various sources were treated with 2,3-butanedione and their bicarbonate dehydration reactions followed. The specific activities of human and bovine CA I and CA II and chicken CA III were not affected by the butanedione treatment, whereas the activities of human, gorilla, and bovine CA III were rapidly activated. These findings suggest that one, or both, of the two arginyl residues which appear to be unique to the active sites of the mammalian CA III isozymes are modified by butanedione.

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