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Thermal Transitions of Myosins/Subfragments from Black Marlin (Makaira mazara) Ordinary and Dark Muscles
Author(s) -
LO JENGREN,
MOCHIZUKI YOSHINORI,
NAGASHIMA YUJI,
TANAKA MUNEHIKO,
ISO NAOMICHI,
TAGUCHI TAKESHI
Publication year - 1991
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.1365-2621.1991.tb14614.x
Subject(s) - myosin , differential scanning calorimetry , chemistry , crystallography , physics , biochemistry , thermodynamics
Thermal transitions were studied by means of differential scanning calorimetry (DSC) and a spectrophotometric method. Three endothermic peaks (40, 43, 50°C: ordinary muscle; 46, 54, 62°C: dark muscle) were observed in DSC thermograms of both myosins. Thermograms of S‐l fragments showed one peak (41°C: ordinary muscle, 43°C: dark muscle). But ordinary and dark muscle rod fragments gave two peaks (41, 62°C) and one peak (58°C), respectively. The spectrophotometric results also showed two thermal transitions for both myosins and one transition for their S‐1 fragments. However, the rod from ordinary muscle myosin had two transitions, whereas that from dark muscle myosin had one transition.