di Bello C, Tonellato M, Lucchiari A, Buso O, Gozzini L, Vita C
Institute of Industrial Chemistry, University of Padua, Italy.
Int J Pept Protein Res. 1990 Apr;35(4):336-45. doi: 10.1111/j.1399-3011.1990.tb00058.x.
The peptide corresponding to the (66-104) sequence of horse heart cytochrome c and its carboxyamide analog, selectively modified at the critical Met80 residue, have been synthesized by stepwise solid-phase methods on PAM and BHA resins respectively. The correctness of the growing peptide chain as well as the homogeneity of the final products have been monitored by several analytical methods including quantitative Edman degradation. After HF cleavage both peptides were purified by semipreparative HPLC. The overall yields were 24% for the native (66-104) and 10% for the carboxyamide analog. The homogeneity of the purified synthetic peptides have been determined by different criteria including HPLC, amino acid composition, Edman degradation, electrophoresis, and tryptic peptide mapping. The synthetic fragments have been utilized for preliminary semisynthesis experiments with the native [Hse greater than 65] (1-65)H heme-sequence.
分别在PAM树脂和BHA树脂上通过逐步固相法合成了与马心脏细胞色素c的（66 - 104）序列相对应的肽及其在关键的Met80残基处选择性修饰的羧酰胺类似物。通过包括定量埃德曼降解在内的几种分析方法监测了不断增长的肽链的正确性以及最终产物的均一性。在氢氟酸裂解后，两种肽都通过半制备高效液相色谱法进行了纯化。天然的（66 - 104）肽的总产率为24%，羧酰胺类似物的总产率为10%。通过包括高效液相色谱法、氨基酸组成分析、埃德曼降解、电泳和胰蛋白酶肽图谱分析等不同标准确定了纯化的合成肽的均一性。合成片段已用于与天然的[Hse大于65]（1 - 65）H血红素序列进行初步半合成实验。
