Parris D, Swart L S
Biochem J. 1975 Mar;145(3):459-67. doi: 10.1042/bj1450459.
The complete amino acid sequence of mohair protein, SCMKB-M1.2 (97 residues), was determined. The protein was isolated from reduced and carboxymethylated mohair by chromatography on DEAE-cellulose phosphate. Peptides for sequence determination were obtained by digestion with trypsin, pepsin, chymotrypsin, thermolysin and papain, and were fractionated by DEAE-cellulose chromatography, paper chromatography and electrophoresis. The sequence of the peptides were determined by the Edman degradation method (by use of both the Beckman Sequence and a non-automatic procedure), and by partial acid hydrolysis. The protein is closely homologous to wool protein SCMKB-IIIB2, and also contains acetylated alanine as N-terminal amino acid.
测定了马海毛蛋白SCMKB - M1.2(97个残基)的完整氨基酸序列。该蛋白是通过在磷酸二乙氨基乙醇纤维素上进行色谱分离,从还原和羧甲基化的马海毛中分离得到的。用于序列测定的肽段通过用胰蛋白酶、胃蛋白酶、胰凝乳蛋白酶、嗜热菌蛋白酶和木瓜蛋白酶消化获得,并通过二乙氨基乙醇纤维素色谱、纸色谱和电泳进行分级分离。肽段的序列通过埃德曼降解法(同时使用贝克曼序列仪和非自动程序)以及部分酸水解来确定。该蛋白与羊毛蛋白SCMKB - IIIB2密切同源,并且其N端氨基酸为乙酰化丙氨酸。