Drøhse H B, Foltmann B
Institute of Biochemical Genetics, University of Copenhagen, Denmark.
Biochim Biophys Acta. 1989 May 1;995(3):221-4. doi: 10.1016/0167-4838(89)90039-3.
Limited proteolysis of bovine kappa-casein has been investigated with porcine pepsin A and C, and with the 2 microbial proteinases Mucor miehei proteinase and Endothia parasitica proteinase. The liberated C-terminal glycomacropeptide of kappa-casein was isolated after precipitation in 3% trichloroacetic acid followed by high-performance gel-permeation chromatography on a TSK G3000 SW column. From amino acid analyses and N-terminal sequencing of the liberated peptide it is concluded that porcine pepsin A, C and Mucor miehei proteinase cleave the same bond as chymosin: Phe-105-Met-106 whereas Endothia parasitica proteinase cleaves the bond Ser-104-Phe-105.
利用猪胃蛋白酶A和C以及两种微生物蛋白酶米黑毛霉蛋白酶和寄生内座壳蛋白酶，对牛κ-酪蛋白的有限水解进行了研究。κ-酪蛋白释放出的C端糖巨肽在3%三氯乙酸中沉淀，然后在TSK G3000 SW柱上进行高效凝胶渗透色谱分离后得到分离。通过对释放肽的氨基酸分析和N端测序得出结论，猪胃蛋白酶A、C和米黑毛霉蛋白酶切割的键与凝乳酶相同：苯丙氨酸-105-甲硫氨酸-106，而寄生内座壳蛋白酶切割的键是丝氨酸-104-苯丙氨酸-105。
