[马铃薯蛋白酶蛋白抑制剂中酪氨酸残基的修饰]
[Modification of tyrosine residues in the protein inhibitor of potato proteinases].
作者信息
Dronova L A, Shul'mina A I, Mosolov V V
出版信息
Biokhimiia. 1980 Feb;45(2):285-9.
Treatment of a native protein inhibitor of proteinases by tetranitromethane results inmodification of 3 (out of 8) tyrosine residues in each of the two subunits within the inhibitor molecule. Nitration of surface tyrosines does not change the corformation of the protein and has no effect on its ability to inhibit chymotrypsin. At the same time the tetranitromethane-treated inhibitor possesses a decreased activity with respect to trypsin. In the presence of 0,5 M DS-Na practically all tyrosine residues of the protein are nitrated.
用四硝基甲烷处理蛋白酶的天然蛋白质抑制剂，会使抑制剂分子中两个亚基各自的8个酪氨酸残基中的3个发生修饰。表面酪氨酸的硝化不会改变蛋白质的构象，也不会影响其抑制胰凝乳蛋白酶的能力。同时，经四硝基甲烷处理的抑制剂对胰蛋白酶的活性降低。在0.5M十二烷基硫酸钠存在的情况下，该蛋白质的几乎所有酪氨酸残基都会被硝化。
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