The use of ninhydrin as a reagent for the reversible modification of arginine residues in proteins.
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ABSTRACT:
SUBMITTER: Chaplin MF
PROVIDER: S-EPMC1172855 | biostudies-other | 1976 May
REPOSITORIES: biostudies-other
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Project description:myo-Inositol monophosphatase is inhibited by the arginine-specific reagent phenylglyoxal. The rate of inactivation is decreased in the presence of Pi, a competitive inhibitor of the enzyme. The effect of Pi is dependent on the presence of Mg2+, but is unaffected by Li+, an uncompetitive inhibitor. In the absence of Mg2+, the substrate, Ins(1)P, binds to the enzyme but is not converted into products, and affords only a small degree of protection against inactivation by phenylglyoxal. Li+ had no further effect under these conditions, but in the presence of Mg2+ caused a marked potentiation of the protective effect of substrate alone. In the absence of substrate, Li+ had no effect on activation by phenylglyoxal. Incorporation of 14C-labelled phenylglyoxal showed that inactivation was associated with modification of a single arginine residue per monomer in the dimeric enzyme. These findings support a mechanism in which Li+ inhibits monophosphatase by trapping a phosphorylated enzyme intermediate and preventing its hydrolysis.
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