Jakobsson I, Borulf S, Lindberg T, Benediktsson B
J Pediatr Gastroenterol Nutr. 1983 Nov;2(4):613-6. doi: 10.1097/00005176-198311000-00007.
The hydrolysis of bovine alpha-lactalbumin, beta-lactoglobulin, and casein by human anodal and cathodal trypsins and elastases was studied with the aid of electroimmunoassay and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The rate of hydrolysis of the various proteins by cathodal elastase exceeded that by anodal or cathodal trypsin and anodal elastase. Casein was hydrolyzed more efficiently than alpha-lactalbumin or beta-lactoglobulin. The hydrolysis of the three proteins occurred at a considerably slower rate when present in crude form, as in cow's milk, than when in purified form.
借助电免疫测定法和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳，研究了人阳极和阴极胰蛋白酶及弹性蛋白酶对牛α-乳白蛋白、β-乳球蛋白和酪蛋白的水解作用。阴极弹性蛋白酶对各种蛋白质的水解速率超过阳极或阴极胰蛋白酶及阳极弹性蛋白酶。酪蛋白比α-乳白蛋白或β-乳球蛋白更易被水解。当这三种蛋白质以粗制形式（如在牛奶中）存在时，其水解速率比以纯化形式存在时要慢得多。
