

Author: Bandyopadhyay U. Kaiser T. Rudolf M.T. Schultz C. Guse A.H. Mayr G.W.
Publisher: Elsevier
ISSN: 0006-291X
Source: Biochemical and Biophysical Research Communications, Vol.240, Iss.1, 1997-11, pp. : 146-149
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Abstract
Inositol 1,2,3,5,6-pentakisphosphate (Ins(1,2,3,5,6)P5) 5-phosphatase present in fetal calf thymus has been partially purified. This enzyme was inhibited dose-dependently by different thiol modifiers like N-ethylmaleimide (NEM), p-chloromercuribenzene sulfonate (PCMBS), diamide, and phenylarsine oxide (PAO). The inhibition by PCMBS and diamide was protected by preincubation with dithiothreitol (DTT) and the phosphatase substrate, Ins(1,2,3,5,6)P5. Diamide, a compound that specifically modifies vicinal thiol groups, also blocked the 5-phosphatase dose-dependently. Specificity of this blockade was proven by using dimercaptopropanol (DMP), a compound known to protect vicinal thiol groups. DMP prevented the enzyme from inhibition by diamide. These data suggest that vicinal thiols are involved in Ins(1,2,3,5,6)P5 5-phosphatase activity. Copyright 1997 Academic Press.
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