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  • Title: Acylation and carbamylation of equine muscle carbonic anhydrase (CA-III) upon reaction with p-nitrophenyl esters and carbamoyl phosphate.
    Author: Nishita T, Deutsch HF.
    Journal: Int J Biochem; 1986; 18(4):319-25. PubMed ID: 3086146.
    Abstract:
    Equine muscle carbonic anhydrase (CA-III) behaves like ubiquitin in undergoing extensive acylation of N epsilon-lysine residues upon reacting with p-nitrophenyl esters. The enzyme undergoes extensive carbamoylation of lysine residues when reacted with carbamoyl phosphate. The modification of from 6 to 7 lysine residues results in the production of a series of more anodic electrophoretic components. The derivatization of the lysine residues leads to a marked decrease in the enzyme's ability to hydrate CO2. The equine CA-III possesses both acid and alkaline phosphatase activities in contrast to the rabbit which possesses only the former type.
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