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Purification and properties of human erythrocyte inosine triphosphate pyrophosphohydrolase
Author(s) -
Vanderheiden Bernardo S.
Publication year - 1979
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1040980106
Subject(s) - enzyme , biochemistry , chemistry , inosine , specific activity , glycine , amino acid
Inosine triphosphate pyrophosphohydrolase from human erythrocytes was purified and characterized. The enzyme is highly specific for ITP and shows optimal activity in glycine buffer pH 9.6 and 50 mM MgCl 2 . The K m of the enzyme is 1.3 × 10 −4 , the V max = 1.2 × 10 −9 and the K eq = 3.8 × 10 4 . Human erythrocyte ITP pyrophosphohydrolase does not require SH compounds for activation. The enzyme is inhibited by Cd ++ , Co ++ , and Ca ++ ions and by phydroxymercuribenzoate.