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Titolo:
Biological activity of single chain chorionic gonadotropin, hCG alpha beta, is decreased upon deletion of five carboxyl terminal amino acids of the alpha subunit without affecting its receptor binding
Autore:
Sen Gupta, C; Dighe, RR;
Indirizzi:
Indian Inst Sci, Dept Mol Reprod Dev & Genet, Bangalore 560012, Karnataka,India Indian Inst Sci Bangalore Karnataka India 560012 560012, Karnataka,India
Titolo Testata:
JOURNAL OF MOLECULAR ENDOCRINOLOGY
fascicolo: 2, volume: 24, anno: 2000,
pagine: 157 - 164
SICI:
0952-5041(200004)24:2<157:BAOSCC>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
FOLLICLE-STIMULATING-HORMONE; GLYCOPROTEIN HORMONES; MONOCLONAL-ANTIBODIES; LINKER SEQUENCE; CG-BETA; EXPRESSION; COMMON; CHORIOGONADOTROPIN; FOLLITROPIN; BIOACTIVITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Dighe, RR Indian Inst Sci, Dept Mol Reprod Dev & Genet, Bangalore 560012, Karnataka,India Indian Inst Sci Bangalore Karnataka India 560012 arnataka,India
Citazione:
C. Sen Gupta e R.R. Dighe, "Biological activity of single chain chorionic gonadotropin, hCG alpha beta, is decreased upon deletion of five carboxyl terminal amino acids of the alpha subunit without affecting its receptor binding", J MOL ENDOC, 24(2), 2000, pp. 157-164

Abstract

The strategy of translationally fusing the two subunits of human chorionicgonadotropin (hCG) has been used to produce recombinant single chain hCG in which the C-terminus of the alpha subunit is fused to the N-terminus betawithout any linker using Pichia pastoris expression system. The Pichia-expressed hCG alpha beta (phCG alpha beta) attained an overall conformation similar to that of hCG, and could bind to the receptor and elicit biological response, suggesting that receptor binding and signal transduction can takeplace even with a molecule having blocked the C-terminus of the alpha subunit. The carboxyl terminal of the alpha subunit has been shown to be involved in hormone binding and signal transduction of all the heterodimeric glycoprotein hormones. However, deletion of five amino acids from the C-terminus of the alpha subunit in the single chain hCG did not alter the overall conformation of the fusion molecule and its receptor binding ability, but ledto a significant reduction in its ability to elicit biological response. These data show that these five amino acids at the C-terminus of the a subunit in the single chain hCG are not absolutely essential for attaining a conformation required for receptor binding, but are essential for obtaining a full biological response.

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Documento generato il 10/07/20 alle ore 15:59:35