✦ LIBER ✦

Purification and properties of human erythrocyte inosine triphosphate pyrophosphohydrolase

✍ Scribed by Bernardo S. Vanderheiden

Publisher: John Wiley and Sons
Year: 1979
Tongue: English
Weight: 468 KB
Volume: 98
Category: Article
ISSN: 0021-9541
DOI: 10.1002/jcp.1040980106

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✦ Synopsis

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 MgC1,. The K, of the enzyme is 1.3 x and the Kq = 3.8 x lo4.

Human erythrocyte ITP pyrophosphohydrolase does not require SH compounds for activation. The enzyme is inhibited by Cd", Co", and Ca++ ions and by phydroxymercuribenzoate. the V, , , = 1.2 x METHODS

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