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Inhibition of the activity of aminoacyl‐tRNA synthetases in pollen grains of maize
Author(s) -
Radlowski Marek,
Bartkowiak Slawomir,
Krolikowski Zygmunt
Publication year - 1993
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1993.tb01350.x
Subject(s) - pronase , sephadex , biochemistry , aminoacyl trna synthetase , aminoacylation , enzyme , specific activity , affinity chromatography , molecular mass , enzyme assay , enzyme kinetics , biology , chemistry , michaelis–menten kinetics , column chromatography , amino acid , chromatography , transfer rna , active site , trypsin , rna , gene
Extracts from pollen grains of maize ( Zea mays L.) show a low activity of aminoacyltRNA synthetases (EC 6. 1. 1). They also contain a specific factor inhibiting the activity of these enzymes. The molecular mass of this factor, which may be a short peptide, is about 3000 Da as determined by column chromatography on Sephadex G‐25 Fine. The Michaelis constant (K m ), determined for the amino acid in the presence of this factor, suggests its allosteric influence on the affinity of the enzyme. Short‐term incubation of the factor with pronase R resulted in conversion of the inhibiting action into a stimulating one. Kinetics of aminoacylation reactions confirm inhibitory and stimulative influences of the effector on the enzyme activity. High performance liquid chromatography shows that inhibition of the activity of aminoacyl‐tRNA synthetases is affected by a group of compounds of similar molecular masses.