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Hydrophobic fluorescent group coupled to Taka‐amylase A. Change of its environment accompanying splitting of disulfide bonds
Author(s) -
Takagi Toshio,
Nakanishi Yoshiko,
Okabe Nobuo,
Isemura Toshizo
Publication year - 1967
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1967.360050704
Subject(s) - chemistry , disulfide bond , fluorescence , amylase , cleavage (geology) , polymer chemistry , sulfonyl , organic chemistry , photochemistry , stereochemistry , biochemistry , enzyme , physics , geotechnical engineering , quantum mechanics , fracture (geology) , engineering , alkyl
Native Taka‐amylase A (α‐amylase produced by Asp. oryzae ) was coupled with 1‐dimethylaminonaphthalene‐5‐sulfonyl chloride. When disulfide bonds of the modified enxyme were split by reduction or by reduction and subsequent carboxymethylation, its fluorescent properties changed markedly. It was suggested that the hydrophobic dye group is incorporated into a hydrophobic region as the consequence of the flexibility gained by the polypeptide chain by the cleavage of disulfide bonds.