Solubility of the proteins of mackerel light muscle at low ionic strength

被引:24
作者
Feng, YM [1 ]
Hultin, HO [1 ]
机构
[1] Univ Massachusetts, Marine Stn, Dept Food Sci, Massachusetts Agr Expt Stn, Gloucester, MA 01930 USA
关键词
D O I
10.1111/j.1745-4514.1997.tb00201.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Over 90% of the proteins of mackerel light muscle were soluble in solutions of physiological ionic strength or less. To accomplish this solubilization, 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), alpha-actinin (95 kDa) and desmin (56 kDa).
引用
收藏
页码:479 / 496
页数:18
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