Acharya A S, Di Donato A, Manjula B N, Fischetti V A, Manning J M
Int J Pept Protein Res. 1983 Jul;22(1):78-82. doi: 10.1111/j.1399-3011.1983.tb02071.x.
The tryptic peptides of the aminoethylated alpha- and beta-chain of hemoglobin have been separated on a Partisil-10 ODS-2 column with a linear gradient of acetonitrile containing 0.1% trifluoroacetic acid. The elution profile of the tryptic peptides of the chains obtained with this acetonitrile trifluoroacetate system has been compared with that obtained using phosphoric acid as the ion-pairing reagent. This comparison demonstrated that trifluoroacetate influences the retention times of the histidine-containing tryptic peptides much more than it affects those peptides that do not contain histidine residues. This behavior has been rationalized on the basis of ion-pairing of trifluoroacetate with the histidine residues of the tryptic peptides.
血红蛋白氨乙基化α链和β链的胰蛋白酶肽段,已在Partisil - 10 ODS - 2柱上,用含0.1%三氟乙酸的乙腈线性梯度进行分离。已将用该乙腈三氟乙酸盐体系获得的链的胰蛋白酶肽段洗脱图谱,与使用磷酸作为离子对试剂获得的洗脱图谱进行了比较。该比较表明,三氟乙酸盐对含组氨酸的胰蛋白酶肽段保留时间的影响,远大于对不含组氨酸残基的肽段的影响。这种行为已根据三氟乙酸盐与胰蛋白酶肽段的组氨酸残基的离子对作用得到了合理的解释。