Bingham E W
J Dairy Sci. 1975 Jan;58(1):13-8. doi: 10.3168/jds.S0022-0302(75)84510-3.
The action of rennin on kappa-casein was studied as a function of time using several methods to measure activity. The first indication of rennin cleavage of kappa-casein is precipitability in .1 M acetate buffer at pH 5.2 and 5 C. A longer exposure to rennin is required to alter kappa-casein so that it forms a precipitate with calcium ions and loses its ability to stabilize alpha s-casein. The least sensitive indication of rennin activity is measurement of nitrogen soluble in 2% trichloroacetic acid. Electrophoresis experiments showed that these methods detect various stages in the conversion of kappa-casein para-kappa-casein.
使用几种方法测量活性,研究了凝乳酶对κ-酪蛋白的作用随时间的变化。凝乳酶切割κ-酪蛋白的第一个迹象是在pH 5.2和5℃的0.1M醋酸盐缓冲液中的沉淀性。需要更长时间暴露于凝乳酶才能改变κ-酪蛋白,使其与钙离子形成沉淀并失去稳定αs-酪蛋白的能力。凝乳酶活性最不敏感的指标是测量可溶于2%三氯乙酸的氮。电泳实验表明,这些方法检测到了κ-酪蛋白向对-κ-酪蛋白转化的不同阶段。