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Updated: Jul 10, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins
M Chaijan1, S Benjakul, W Visessanguan
1Dept. of Food Technology, Faculty of Agro-Industry, Prince of Songkla Univ., Hat Yai, 90112, Thailand.
Abstract:
The effects of ionic strength (0, 0.3, and 0.6 M KCl) and temperature (4 and 25 degrees C) on the interaction between fish myoglobin and myofibrillar proteins were investigated in a model system. Increases in the relative content of bound myoglobin and metmyoglobin formation in myoglobin-natural actomyosin (NAM) mixtures with concurrent decreases in whiteness and Ca(2+)-ATPase activity were observed with increasing ionic strength (P < 0.05). The relative content of bound myoglobin and the oxidation of oxymyoglobin were generally greater at 25 degrees C than at 4 degrees C (P < 0.05). Binding of myoglobin to NAM resulted in decreased whiteness (P < 0.05). Ca(2+)-ATPase was not affected by temperature (P > 0.05). SDS-PAGE patterns of protein samples suggested that myoglobin-NAM interactions did not involve disulfide bonds. The formation of high-molecular-weight aggregates (>206 kDa) was observed and was more pronounced at higher ionic strength and higher temperature.
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