结蛋白
标签
长春新碱
蛋白质丝
最长肌
温柔
中间灯丝
解剖
化学
生物
生物化学
细胞骨架
食品科学
免疫学
免疫组织化学
细胞
波形蛋白
作者
E H Morrison,Martin M. Mielche,Peter P. Purslow
出处
期刊:Meat Science
[Elsevier]
日期:1998-09-01
卷期号:50 (1): 91-104
被引量:62
标识
DOI:10.1016/s0309-1740(98)00019-9
摘要
Two intermediate filament proteins, desmin and vinculin, were immunofluorescently localised in porcine longissimus dorsi∗∗ and iliocostalis muscles up to 7 days post mortem. Changes in tenderness of the m. longissimus and the water-holding capacity of both muscles were also monitored throughout this storage period. Longissimus muscle shows a rapid decline in the overall intensity of labelling for both desmin and vinculin. In contrast to the vinculin labelling, desmin labelling is preferentially lost from type IIB muscle fibres in the longissimus muscle. In the redder iliocostalis muscle, the loss of desmin and vinculin labelling was less rapid and did not show an obvious relation to muscle fibre type. In one sample with very high water loss, there were indications of greater extracellular space development and delayed loss of intermediate filament labelling. The time course of diminishing intermediate filament labelling is consistent with previous suggestions that degradation of these proteins is involved in post-mortem conditioning. The variations within and between muscles shown here may explain some of the variability in their mechanical properties. Additionally, it is suggested that intermediate filament integrity is necessary for the expulsion of water from the muscle cells during drip formation.
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