Kinetic characterization of bovine lung low-molecular-weight protein tyrosine phosphatase.

Abstract:

:Protein tyrosine phosphatase is an important class of enzymes that plays an essential role in the cellular proliferation, differentiation, and oncogenesis. In this paper we report characterization of a low-molecular-weight protein tyrosine phosphatase purified from bovine lung. The enzyme activity was essentially independent of metal ions and sensitive to sulfhydryl reagents. Both vanadate and inorganic phosphate are competitive inhibitors, with Ki values of 0.38 microM and 0.28 mM, respectively. Besides p-nitrophenyl phosphate, the enzyme was also able to efficiently hydrolyze tyrosine phosphate, beta-naphthyl phosphate, and flavine mononucleotide.

journal_name

Exp Lung Res

authors

Buzalaf MA,Taga EM,Granjeiro JM,Ferreira CV,Lourenção VA,Ortega MM,Poletto DW,Aoyama H

doi

10.3109/01902149809041534

subject

Has Abstract

pub_date

1998-05-01 00:00:00

pages

269-72

issue

3

eissn

0190-2148

issn

1521-0499

journal_volume

24

pub_type

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