Stewart D I, Golosinska K, Smillie L B
FEBS Lett. 1983 Jun 27;157(1):129-32. doi: 10.1016/0014-5793(83)81130-2.
A tropomyosin-binding protein (app. Mr 17000) was detected in equine platelet preparations by a gel overlay technique. Its isolation, amino acid and partial sequence analyses have shown it to be histone H2B. As with a similar protein from pig platelet preparations [der Terrossian et al. (1983) FEBS Lett. 152, 202-206], it inhibits Mg2+-dependent actomyosin S1 ATPase. This inhibition is partially reversed in the presence of calmodulin and Ca2+ but is not potentiated, unlike troponin-I, by tropomyosin. This protein, along with the other histones, is almost certainly derived from a low level of contaminating nucleated cells in most platelet preparations.
通过凝胶覆盖技术在马血小板制剂中检测到一种原肌球蛋白结合蛋白（表观分子量17000）。其分离、氨基酸和部分序列分析表明它是组蛋白H2B。与来自猪血小板制剂的类似蛋白[德尔·特罗西安等人（1983年）《欧洲生物化学学会联合会快报》152卷，202 - 206页]一样，它抑制Mg2 +依赖性肌动球蛋白S1 ATP酶。在钙调蛋白和Ca2 +存在的情况下，这种抑制作用部分逆转，但与肌钙蛋白I不同，原肌球蛋白不会增强这种抑制作用。这种蛋白质与其他组蛋白几乎肯定来自大多数血小板制剂中低水平的污染有核细胞。
