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Fast dissociation of phe‐tRNA synthetase from Aspergillus nidulans immobilized on sepharose‐6B column by NaCl
Author(s) -
Singh Nalin Kumar,
Tiwary Bhupendra N.
Publication year - 1996
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620360112
Subject(s) - sepharose , dissociation (chemistry) , chemistry , covalent bond , elution , aspergillus nidulans , enzyme , affinity chromatography , ligand (biochemistry) , chromatography , molecule , adsorption , agarose , phenylalanine , stereochemistry , biochemistry , organic chemistry , amino acid , receptor , mutant , gene
Phenylalanyl‐tRNA 2 ) synthetase from Aspergillus nidulans was efficiently immobilised to sepharose 6B column containing phenylalanine as the ligand. NaCl was found to be a potent dissociating agent for the immobilised enzyme. While 0.5 M NaCl in discontinuous elution showed a slow impetus on dissociation giving a plateaux profile, a solution of 0.8 M NaCl made the eiution rapid giving a sharp peak. On the other hand, in a gradient (continuous) elution the rapidity of dissociation was found to be enhanced with the increase in the difference of the two concentrations. The result suggests that Na + ions interact with the protein binding site of the ligand eventually dissociating the enzyme molecule by disrupting the covalent bond without affecting its normal catalytic activity.