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胃蛋白酶引发κ-酪蛋白凝固的动力学

Kinetics of pepsin-initiated coagulation of kappa-casein.

作者信息

Hyslop D B, Richardson T, Ryan D S

出版信息

Biochim Biophys Acta. 1979 Feb 9;566(2):390-6. doi: 10.1016/0005-2744(79)90043-3.

DOI:10.1016/0005-2744(79)90043-3
PMID:369612
Abstract

The kinetics of pepsin initiated coagulation of kappa-casein have been studied at pH 5.8. The primary and secondary phases of coagulation are shown to proceed simultaneously. The theory of enzymatically initiated clotting reactions proposed by Payens (Payens, T.A.J. (1976) Neth. Milk Dairy J. 30, 55--59) has been applied to this clotting system and has been used to obtain rate constants for the secondary phase of coagulation. As expected, clotting rate constants for kappa-casein increase with pepsin concentration. An activation energy of 30.6 kcal/mol has been obtained for the secondary phase of coagulation. Turbidity measurements are a convenient means for studying the secondary phase of coagulation but do not provide an unambiguous means for studying the primary phase of the reaction.

摘要

已在pH 5.8条件下研究了胃蛋白酶引发κ-酪蛋白凝固的动力学。结果表明,凝固的初级阶段和次级阶段是同时进行的。Payens提出的酶促引发凝血反应理论(Payens, T.A.J. (1976) Neth. Milk Dairy J. 30, 55--59)已应用于该凝血系统,并用于获得凝固次级阶段的速率常数。正如预期的那样,κ-酪蛋白的凝血速率常数随胃蛋白酶浓度的增加而增加。已获得凝固次级阶段的活化能为30.6千卡/摩尔。浊度测量是研究凝固次级阶段的便捷手段,但不是研究反应初级阶段的明确手段。

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