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Genetic basis of inosine triphosphate pyrophosphohydrolase deficiency

โœ Scribed by Sumi, Satoshi; Marinaki, Anthony; Arenas, Monica; Fairbanks, Lynette; Shobowale-Bakre, Monsor; Rees, David; Thein, Swee; Ansari, Azhar; Sanderson, Jeremy; De Abreu, Ronney


Book ID
113043548
Publisher
Springer
Year
2002
Tongue
English
Weight
399 KB
Volume
111
Category
Article
ISSN
0340-6717

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Purification and properties of human ery
โœ Bernardo S. Vanderheiden ๐Ÿ“‚ Article ๐Ÿ“… 1979 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 468 KB

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 pyrophosphohydrola