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Protein‐Protein Interaction of Fish Myosin Fragments
Author(s) -
TAGUCHI TAKESHI,
ISHIZAKA HIROSHI,
TANAKA MUNEHIKO,
NAGASHIMA YUJI,
AMANO KEISHI
Publication year - 1987
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1987.tb14287.x
Subject(s) - heavy meromyosin , myosin , fish <actinopterygii> , chemistry , absorbance , meromyosin , biophysics , biochemistry , fishery , biology , myosin light chain kinase , chromatography , myosin head
Protein‐protein interaction of myosin fragments from flying fish and white marlin muscles was studied by means of absorbance changes resulting from aggregation at temperatures of 20°C to 70°C. Subfragment‐1 (S‐1) exhibited a high extent of interaction with the transition temperature of 35–36°C, while the interaction of heavy meromyosin (HMM) was very weak. Though light meromyosin (LMM) gave lower interaction values throughout the heating temperature, the addition of butanol promoted markedly the interactions at the temperature above 50°C. The degree of promotion was high for flying fish and low for white marlin.