Castberg H B, Egelrud T, Solberg P, Olivecrona T
J Dairy Res. 1975 Jun;42(2):255-66. doi: 10.1017/s0022029900015296.
The lipoprotein lipase and tributyrate hydrolysing activities were found to be similarly distributed in the fractions obtained when whole milk was separated into skim-milk and cream, and when the cream was washed and freed from lipid. These enzyme activities in skim-milks and in extracts of lipid-free cream could not be separated by affinity chromatography on heparin-Sepharose. The enzymes were inactivated to the same degree when incubated at 37 degrees C in the presence of 1-5 M-NaCl, pH 8-5, and both showed marked decrease in stability at 4 degrees C in UV-light caused the same decrease in both lipoprotein lipase and tributyrate hydrolysing activities. An antiserum against a highly purified skim-milk lipoprotein lipase caused total inhibition of the lipoprotein lipase and tributyrate hydrolysing activities in skim-milk and in extracts of lipid-free cream. It is suggested that in bovine milk there is only one major lipase and that it is identical to lipoprotein lipase.
当全脂牛奶分离成脱脂牛奶和奶油，以及奶油经过洗涤并去除脂质后，脂蛋白脂肪酶和丁酸水解活性在得到的各组分中的分布相似。脱脂牛奶和无脂奶油提取物中的这些酶活性，不能通过肝素琼脂糖亲和层析分离。当在37℃、pH 8.5且存在1 - 5 M氯化钠的条件下孵育时，这两种酶被灭活的程度相同，并且在4℃时二者的稳定性均显著下降，紫外线照射导致脂蛋白脂肪酶和丁酸水解活性出现相同程度的降低。一种针对高度纯化的脱脂牛奶脂蛋白脂肪酶的抗血清，可完全抑制脱脂牛奶和无脂奶油提取物中的脂蛋白脂肪酶和丁酸水解活性。研究表明，牛乳中只有一种主要的脂肪酶，且它与脂蛋白脂肪酶相同。
