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SOLUBILITY OF THE PROTEINS OF MACKEREL LIGHT MUSCLE AT LOW IONIC STRENGTH
Author(s) -
FENG YUMING,
HULTIN HERBERT O.
Publication year - 1997
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1997.tb00201.x
Subject(s) - myofibril , ionic strength , chemistry , desmin , cytoskeleton , solubility , mackerel , biochemistry , sodium , biophysics , chromatography , aqueous solution , biology , fishery , fish <actinopterygii> , vimentin , immunohistochemistry , organic chemistry , cell , immunology
Over 90% of the proteins of mackerel light muscle were soluble in solutions of physiological ionic strength or less. To accomplish this solublization, it was necessary to extract certain proteins at moderate ionic strength and neutral pH before extracting the rest of the myofibrillar and cytoskeletal proteins in water. Six proteins were favorably solubilized by sodium chloride solutions of moderate ionic strength at neutral pH under conditions that allowed later dissolution of myofibrillar and cytoskeletal proteins in water. The possibility is suggested that three of these proteins were involved in preventing the solubilization in water of other myofibrillar and cytoskeletal proteins of mackerel light muscle. Based on molecular masses and relative abundance, these proteins could possibly be M‐protein (166 kDa), α‐actinin (95 kDa) and desmin (56 kDa).