PURIFICATION AND CHARACTERIZATION OF AN ACID-PHOSPHATASE FROM ARACHIS-HYPOGAEA

Authors
SRIVASTAVA R RAJPUT YS KHARE SK TYAGI R GUPTA MN
Citation
R. Srivastava et al., PURIFICATION AND CHARACTERIZATION OF AN ACID-PHOSPHATASE FROM ARACHIS-HYPOGAEA, Biochemistry and molecular biology international, 35(5), 1995, pp. 949-956
Citations number
19
Categorie Soggetti
Biology
Journal title
Biochemistry and molecular biology international → ACNP
ISSN journal
10399712
Volume
35
Issue
5
Year of publication
1995
Pages
949 - 956
Database
ISI
SICI code
1039-9712(1995)35:5<949:PACOAA>2.0.ZU;2-B
Abstract
An acid phosphatase from Arachis hypogaea ( peanuts) has been purified . The electrophoretically homogeneous enzyme preparation is free of an y phophodiesterase activity. The enzyme has a molecular weight of 120, 000. Among the various phosphomonoesters tested, p-nitrophenylphosphat e was found to be its most effective substrate. The K-m for p-nitrophe nylphosphate was 1.21 mM at pH 5.0 and 25 degrees C. The enzyme was th ermostable and did not loose activity after 1 hr at 50 degrees C.