ISSN:
1573-4919
Keywords:
protein phosphatase-1
;
mutagenesis of protein phosphatase-1
;
cysteine residues
;
phosphatase-1
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Abstract We have generated site-directed mutants of the catalytic subunit of rabbit muscle ppase-1. Since it is known that ppase-1 and ppase-2A are highly susceptible to inactivation by sulfhydryl reagents, we have mutagenized the six cysteine residues conserved between these two enzymes to serines. The six mutants were purified to near homogeneity by affinity chromatography on inhibitor-2-Sepharose and characterized. All six exhibited enzymatic activity. These results indicate that the catalytic mechanism of ppase-1 is different from that of the protein tyrosine phosphatases which involve a cysteinyl phosphate intermediate.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01076762
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