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首页> 外文期刊>Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology >Interaction of second and third domains of Japanese quail ovomucoid with ten mammalian trypsins
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Interaction of second and third domains of Japanese quail ovomucoid with ten mammalian trypsins

机译：日本鹌鹑卵类粘蛋白的第二和第三域与十种哺乳动物胰蛋白酶的相互作用

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摘要

Second and third domains were prepared from Japanese quail ovomucoid and association equilibrium constants, k_as, were measured at 25 ℃ and pH 8 for these domains with trypsins from ten mammalian species: cat, cow, dog, guinea pig, hog, horse, man, rabbit, rat, and sheep. The values ranged from 10~8 M~(-1) to 10~(10) M~(-1) for the second domain-trypsin associations and from 10~6 M~(-1) to 10~8 M~(-1) for the third domain-trypsin associations. Changes in K_a values for the interactions between the trypsins and each domain are attributed to slight changes in surface conformation caused by the residue changes in the inhibitor-binding region other than the S_1 pocket of the trypsin species. The representative of such residue changes is assumed to be the one observed at residue 217 of trypsin molecule. Concerning each trypsin, the K_a value with the second domain was always higher than that with the third domain. However, the ratios between the two equilibrium constants varied from 3 to 60 depending upon trypsin species. This means that amino acid changes in enzyme-contact residues other than the P_1 site of the Kazal-type inhibitor can make it possible to recognize even a slight difference in inhibitor-binding surface among the enzymes with the same S_1 pocket and highly similar overall three-dimensional structure.
机译：根据日本鹌鹑卵类粘液蛋白制备第二和第三个域，并用25种胰蛋白酶从10种哺乳动物物种（猫，牛，狗，豚鼠，猪，马，人）在25℃和pH 8下测量缔合平衡常数k_as。兔子，老鼠和绵羊。第二域-胰蛋白酶关联的值的范围从10〜8 M〜（-1）到10〜（10）M〜（-1），从10〜6 M〜（-1）到10〜8 M〜（ -1）用于第三域-胰蛋白酶关联。胰蛋白酶与每个结构域之间相互作用的K_a值的变化归因于表面构象的细微变化，这是由除胰蛋白酶物种的S_1口袋以外的抑制剂结合区域中的残基变化引起的。假定这种残基变化的代表是在胰蛋白酶分子的残基217处观察到的残基变化。对于每个胰蛋白酶，第二个域的K_a值始终高于第三个域的K_a值。但是，取决于胰蛋白酶的种类，两个平衡常数之间的比率在3至60之间变化。这意味着，除了Kazal型抑制剂的P_1位点以外，酶接触残基中的氨基酸变化可以识别具有相同S_1口袋和高度相似的三种酶的抑制剂结合表面的细微差异。尺寸结构。

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