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

Autor:	Mineo Niwa, Masakazu Kobayashi, Yoshinori Ishii, Kouichi Tamura, Hisashi Yamada, Michio Iwai
Rok vydání:	1999
Předmět:	chemistry.chemical_classification Stereochemistry Chemistry law Protease digestion Protein primary structure Recombinant DNA Disulfide bond Organic chemistry Peptide General Chemistry Protein disulfide-isomerase law.invention
Zdroj:	Bulletin of the Chemical Society of Japan. 72:1827-1835
ISSN:	1348-0634 0009-2673
DOI:	10.1246/bcsj.72.1827
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::be2825f367aa72be9beaf776eb2bc300 https://doi.org/10.1246/bcsj.72.1827 Zobrazit plný text záznamu