Lemieux L, Amiot J
Département de Sciences et Technologie des Aliments, Université Laval, Sainte-Foy, Québec, Canada.
J Chromatogr. 1990 Nov 2;519(2):299-321. doi: 10.1016/0021-9673(90)85160-w.
A mixture of small peptides of molecular weight averaging 1000 daltons, obtained by controlled hydrolysis of casein with proteases, chymotrypsin and trypsin, was separated by size-exclusion and reversed-phase high-performance liquid chromatography. Peptides were identified and located in the known casein structures from their amino acid content and their N- and C-terminal amino acid analyses. The primary structure of peptides identified from casein hydrolysate phosphorylated and casein hydrolysate dephosphorylated is presented.
通过用蛋白酶、胰凝乳蛋白酶和胰蛋白酶对酪蛋白进行可控水解获得的平均分子量为1000道尔顿的小肽混合物,通过尺寸排阻和反相高效液相色谱法进行分离。根据肽的氨基酸含量及其N端和C端氨基酸分析,在已知的酪蛋白结构中鉴定并定位肽。给出了从磷酸化酪蛋白水解产物和去磷酸化酪蛋白水解产物中鉴定出的肽的一级结构。