Fong S L, Hargrave P A
Int J Pept Protein Res. 1977;10(2):139-45. doi: 10.1111/j.1399-3011.1977.tb02787.x.
A method has been developed for selectively preparing the carboxyl-terminal tryptic peptide of proteins by cleavage at arginyl residues. The succinylated protein is digested with trypsin and the peptides produced are maleylated. Maleylated peptides are then submitted to cation-exchange chromatography in urea at low pH and ionic strength. Arginine-containing peptides are retained by the resin. The carboxyl-terminal peptide emerges unretarded and in pure form. This method has been applied to four proteins of known sequence. Yields as high as 88% have been obtained.
已开发出一种通过在精氨酰残基处裂解来选择性制备蛋白质羧基末端胰蛋白酶肽的方法。将琥珀酰化的蛋白质用胰蛋白酶消化，产生的肽进行马来酰化。然后将马来酰化的肽在低pH和离子强度的尿素中进行阳离子交换色谱分析。含精氨酸的肽被树脂保留。羧基末端肽不被阻滞且以纯形式出现。该方法已应用于四种已知序列的蛋白质。已获得高达88%的产率。
