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首页> 外文期刊>American Journal of Physiology >Variations in apparent mass of mammalian fast-type myosin light chains correlate with species body size, from shrew to elephant.
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Variations in apparent mass of mammalian fast-type myosin light chains correlate with species body size, from shrew to elephant.

机译：从sh到大象，哺乳动物快速型肌球蛋白轻链表观质量的变化与物种的体型相关。

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摘要

A recent study (Bicer S and Reiser PJ. J Muscle Res Cell Motil 25: 623-633, 2004) suggested considerable variation in the apparent molecular mass (M(a)), deduced from electrophoretic mobility, in fast-type myosin light chains (MLCF), especially MLC1F, among mammalian species. Furthermore, there was an indication that MLC1F M(a) generally correlates with species body mass, over an approximately 4,000-fold range in body mass. The results also suggested that M(a) of other low-molecular-weight myofibrillar proteins is less variable and not as strongly correlated with body mass among the same species. The objective of this study was to test the hypotheses that the M(a) of MLCs does, in fact, vary and correlate with species body mass. The electrophoretic mobilities of MLCF isoforms from 19 species, varying in size approximately 500,000-fold, were quantitated. The results confirm that the M(a) of MLC1F and MLC2F vary significantly among mammals, spanning a very broad range in body mass; the MLC1F M(a) varies more than that of other low-molecular-weight myofibrillar proteins; and there is a significant correlation between species body mass and MLC1F M(a). Differences in MLC1F M(a) among five species can be accounted for by differences in the reported amino acid sequence, especially the length of a common polyalanine region near the NH(2)-terminal actin-binding site. The possibility that the differences in MLC1F sequence among mammalian species, in and adjacent to the actin-binding region, are related to differences in modulation of cross-bridge kinetics in species with diverse locomotion kinetics is discussed.
机译：最近的一项研究（Bicer S和Reiser PJ。J Muscle Res Cell Motil 25：623-633，2004）表明，在快速型肌球蛋白轻链中，由电泳迁移率推导的表观分子量（M（a））存在很大差异。 （MLCF），尤其是哺乳动物物种中的MLC1F。此外，有迹象表明，MLC1F M（a）通常与物种的体重相关，在大约4,000倍的体重范围内。结果还表明，其他低分子量肌原纤维蛋白的M（a）变异性较小，并且与同一物种中的体重没有很强的相关性。这项研究的目的是检验以下假设：MLC的M（a）实际上确实在变化，并且与物种体重相关。定量分析了来自19个物种的MLCF同工型的电泳迁移率，其大小变化了约500,000倍。结果证实，哺乳动物中MLC1F和MLC2F的M（a）差异很大，其体重范围很广。 MLC1F M（a）的变化比其他低分子量肌原纤维蛋白大;并且物种体重与MLC1F M（a）之间存在显着相关性。五个物种之间的MLC1F M（a）的差异可以通过所报告的氨基酸序列的差异来解释，尤其是靠近NH（2）-末端肌动蛋白结合位点的常见聚丙氨酸区域的长度。讨论了肌动蛋白结合区中和邻近肌动蛋白结合区的哺乳动物物种之间的MLC1F序列差异与具有不同运动动力学的物种中跨桥动力学调制差异有关的可能性。

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