Menegatti E, Guarneri M, Bolognesi M, Ascenzi P, Amiconi G
Dipartimento di Scienze Farmaceutiche, Università di Ferrara, Italy.
J Mol Biol. 1987 Nov 5;198(1):129-32. doi: 10.1016/0022-2836(87)90463-3.
The effect of temperature and pH on the association equilibrium constant (Ka) for the binding of the bovine pancreatic secretory trypsin inhibitor (bovine PSTI, type I; Kazal inhibitor) to bovine beta-trypsin, bovine alpha-chymotrypsin and bovine trypsinogen has been investigated. The results suggest that serine (pro)enzyme inhibitor interaction involves both rigorous spatial configuration and molecular flexibility.
研究了温度和pH对牛胰分泌型胰蛋白酶抑制剂（牛PSTI，I型；卡扎尔抑制剂）与牛β-胰蛋白酶、牛α-胰凝乳蛋白酶和牛胰蛋白酶原结合的缔合平衡常数（Ka）的影响。结果表明，丝氨酸（原）酶抑制剂相互作用涉及严格的空间构型和分子柔韧性。
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