Comparison of calpain susceptibility of various fish myosins in relation to their thermal stabilities.

Abstract

When myosins prepa•¬ed from the skeletal muscles of seven different fish species and rabbit were incubated with calpain in the low salt solution at various temperatures, a myosin rod-like fragment (Mr= 150,000 protein band on SDS-PAGE) was preferentially formed in all myosins examined and increased proportionally to the cleavage of myosin heavy chain. It was found that rabbit myosin, the most thermally stable of myosins was used, the most stable to proteolysis;

Cod (Gadus morhua) Muscle Proteome Cataloging Using 1D-PAGE Protein Separation, Nano-Liquid Chromatography Peptide Fractionation, and Linear Trap Quadrupole (LTQ) Mass Spectrometry

“…The calcium-activated calpain proteases are also involved in fish muscle autolysis. In fish, calpains digest myosin, and it has been shown that calpain activity is higher at low temperatures, suggesting that fish species such as cod that live in cold waters are more susceptible to calpain autolysis (35). As part of our study we identified calpain 1-, calpain 3-, and calpain 5-like proteins.…”

Isolation and Characterization of Calpains From Rainbow Trout Muscle and Their Role in Texture Development

“…Calpains have received a great deal of attention due to their role in (1) muscle protein turnover and growth (Huang and Forsberg 1998) and (2) postmortem proteolysis and the impact on muscle texture (Koohmaraie 1992). However, our knowledge of the calpain system in fish is limited (Muramoto et al. 1989; Toyohara and Makinodan 1989; Nemova et al .…”

“…It is widely accepted that postmortem mammalian muscle tenderization is accelerated through the action of calpains (Koohmaraie 1996). In contrast, fish calpains digest the myosin heavy chain (Muramoto et al 1989). Geesink et al .…”

Proteinases of the calpain family in water invertebrates and fishes

“…Thus, for exam ple, calcium dependent proteinases from skeletal muscles of lobster Homarus americanus cleave myo fibrillar proteins, including actin and myosin [10], calpain like proteinase from octopus Octopus vulgaris degrades the majority of proteins in intact myofibrils, particularly myosin, paramyosin, and actin [14]. Among physiological substrates of calpains from fishes there is a heavy chain of myosin [19]. At the same time, classic µ and m calpains do not cleave actin, slowly hydrolyze myosin, and cleave other myofibril lar proteins in a limited manner forming large frag ments [3].…”