Swarup G, Dasgupta J D, Garbers D L
Adv Enzyme Regul. 1984;22:267-88. doi: 10.1016/0065-2571(84)90018-9.
Tyrosine-specific protein kinases from normal tissue have been studied using synthetic peptides as substrate. Spleen had much higher activity of the enzyme in the particulate fraction than any other normal tissue (except purified T lymphocytes). The tyrosine protein kinase from the particulate fraction of rat spleen was partially purified and characterized. The kinase could phosphorylate src-related as well as unrelated peptides and casein at tyrosine residues. The enzyme in the membrane seemed to have somewhat different substrate specificity than the solubilized, partially purified enzyme. Serum containing antibody to pp60v-src did not precipitate the kinase; however, the protein kinase could phosphorylate the heavy chain of IgG from TBR serum (but not from normal serum). The possible relationship of the tyrosine-specific protein kinase of spleen with pp60c-src and other tyrosine-specific protein kinases is discussed.
已使用合成肽作为底物对来自正常组织的酪氨酸特异性蛋白激酶进行了研究。脾脏颗粒部分的该酶活性比任何其他正常组织（纯化的T淋巴细胞除外）都高得多。对大鼠脾脏颗粒部分的酪氨酸蛋白激酶进行了部分纯化和表征。该激酶可在酪氨酸残基处磷酸化与src相关以及不相关的肽和酪蛋白。膜中的酶似乎与溶解的、部分纯化的酶具有 somewhat 不同的底物特异性。含有抗pp60v-src抗体的血清不会沉淀该激酶；然而，该蛋白激酶可磷酸化来自TBR血清（而非正常血清）的IgG重链。讨论了脾脏酪氨酸特异性蛋白激酶与pp60c-src和其他酪氨酸特异性蛋白激酶之间的可能关系。 （注：原文中“somewhat”未准确翻译出其含义，可能是“有点”“稍微”等意思，需结合上下文进一步确定准确含义。）
