[Changes in the activity and tertiary structure of beta-amylase from wheat seeds under the effect of salts].
Biokhimiia, 1977/12;42(12):2217-20.
Anisimov AA, Aleksapdrova IF, Iudina KA, Abzeev ShK, Kondrat'eva MO, Beresneva GG
PMID: 145880
Abstract
Changes are observed of 1-anylinonaphtalene-8-sulphonate probe fluorescence intensity, connected with beta-amylase in the presence of Ca(NO3)2, Mg(NO3)2, KNO3, NH4NO3 and (NH4)2SO4 at a concentration range within 10(-4)--1 M. Considerable decrease of the fluorescence intensity was observed under the addition of all the salts mentioned at concentration of 10(-3)--10(-4) M. A quantum yield increase of probe fluorescence was noted for Mg(NO3)2 (10(-4) M). High concentrations of Ca(NO3)2 and Mg(NO3)2 (0.25--1 M) also resulted in a sharp increase of the fluorescence intensity. Changes of beta-amylase activity took place simultaneously. The changes of the enzyme activity are suggested to be due to changes in the conformation of the enzyme protein under the effect of salts.
MeSH terms
Amylases; Anilino Naphthalenesulfonates; Kinetics; Macromolecular Substances; Osmolar Concentration; Protein Conformation; Seeds; Spectrometry, Fluorescence; Triticum; beta-Amylase
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