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Characterization of phosphotyrosyl protein phosphatase from the hepatopancreas of the shrimpPenaeus japonicus (Crustacea: Decapoda)

✍ Scribed by Chuang, Nin-Nin ;Wang, Pei-Cheng

Publisher
John Wiley and Sons
Year
1993
Tongue
English
Weight
741 KB
Volume
266
Category
Article
ISSN
0022-104X

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✦ Synopsis

Abstract

Phosphotyrosyl protein phosphatase, purified from the hepatopancreas of Panaeus japonicus, is a monomeric enzyme with a relative mass (Mr) of 28,000, as estimated by size‐exclusion FPLC on a Superose^TM^ 12. It has a hydrophobic domain and can be extracted with the detergent CHAPS. The specific activity of the purified enzyme was 9,800 units/mg of protein. The purified enzyme had an isoelectric point less than 4.6, and an optimal pH of 6.5 with either a synthetic peptide or autophosphorylated receptors for insulin as the substrate. The purified phosphotyrosyl protein phosphatase from shrimp hepatopancreas dephosphorylated human and shrimp receptors for insulin and was inactivated by ZnCl~2~, LiCl, MgCl~2~, and NaF. © 1993 Wiley‐Liss, Inc.

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