Kotts C, Jenness R
J Dairy Sci. 1976 May;59(5):816-22. doi: 10.3168/jds.S0022-0302(76)84281-6.
Kappa-Casein-like proteins were isolated from the milks of cow, goat, reindeer, horse, rat, and rabbit. When treated with rennin, all of the isolated kappa-casein components yielded para-kappa-casein-like bands on gel electrophoresis. The rate of cleavage of these components with rennin was determined by measuring material soluble in trichloroacetic acid (macropeptide). The curves were characteristic of a limited, specific attack by rennin on these proteins. The goat and reindeer kappa-caseins were nearly as bovine kappa-casein, but the cleavage of horse, rat, and rabbit kappa-casein-like components was much slower.
从牛、山羊、驯鹿、马、大鼠和兔子的乳汁中分离出了κ-酪蛋白样蛋白。用凝乳酶处理后,所有分离出的κ-酪蛋白成分在凝胶电泳上都产生了类似副κ-酪蛋白的条带。通过测量三氯乙酸可溶物质(巨肽)来确定这些成分被凝乳酶的裂解速率。这些曲线是凝乳酶对这些蛋白质进行有限的特异性攻击的特征。山羊和驯鹿的κ-酪蛋白与牛κ-酪蛋白几乎一样,但马、大鼠和兔子的κ-酪蛋白样成分的裂解要慢得多。