- Synthesis of two possible disulfide bonds containing peptide fragments (Cys6-Cys47, Cys48-Cys52 (Type I), and Cys6-Cys48, Cys47-Cys52 (Type II) of H-IGF-I) for the identification of disulfide bond linkage in recombinantly produced H-IGF-I
-
The primary structure of human IGF-I, except for the disulfide bond system, has been reported by Rinderknecht and Humbel. IGF-I afforded the corresponding characteristic peptide fragments on V8 protease digestion, which contained Cys6, Cys47, Cys48, and Cys52. Two possible fragments, Type I with Cys6-Cys47 and Cys48-Cys52 and Type II with Cys6-Cys48 and Cys47-Cys52 of h-IGF-I(4-9,47-53), were chemically synthesized. The disulfide bond system of IGF-I was unequivocally determined to be the Type-II form along with Cys18-Cys61. Interestingly, the Type-I system was included in the disulfide bond isomer produced as the main by-product in the refolding step on IGF-I synthesis by the recombinant DNA method.
- Iwai, Michio,Yamada, Hisashi,Ishii, Yoshinori,Tamura, Kouichi,Niwa, Mineo,Kobayashi, Masakazu
-
p. 1827 - 1835
(2007/10/03)
-