Abstract
.kappa.-Casein-like proteins were isolated from the milks of cow [Bos taurus], goat [Capra hircus], reindeer [Rangifer tarandus], horse [Equus caballus], rat [Rattus norvegicus], and rabbit [Oryctolagus cuniculus]. When treated with rennin, all of the isolated .kappa.-casein components yielded para-.kappa.-casein-like bands on gel electrophoresis. The cleavage rate of these components with rennin was determined by measuring material solule 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 sensitive to cleavage by rennin as bovine .kappa.-casein, but the cleavage of horse, rat and rabbit .kappa.-casein-like components was much slower.