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Titolo:
Mapping the receptor binding regions of human chorionic gonadotropin (hCG)using disulfide peptides of its beta-subunit: possible involvement of the disulfide bonds Cys(9)-Cys(57) and Cys(23)-Cys(72) in receptor binding of the hormone
Autore:
Mishra, AK; Mahale, SD; Iyer, KS;
Indirizzi:
Inst Res Reprod, Bombay 400012, Maharashtra, India Inst Res Reprod BombayMaharashtra India 400012 00012, Maharashtra, India
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 1, volume: 58, anno: 2001,
pagine: 17 - 26
SICI:
1397-002X(200107)58:1<17:MTRBRO>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN CHORIOGONADOTROPIN-BETA; HUMAN LUTEINIZING-HORMONE; BIOLOGICAL-ACTIVITY; LH RECEPTOR; PROTEIN; DETERMINANT; ALPHA;
Keywords:
directed synthesis of disulfide peptides; disulfide peptides of the beta-subunit; human chorionic gonadotropin; radioreceptor assay; receptor binding regions; role of disulfide bonds;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Iyer, KS Inst Res Reprod, Jehangir Merwanji St, Bombay 400012, Maharashtra, India Inst Res Reprod Jehangir Merwanji St Bombay Maharashtra India 400012
Citazione:
A.K. Mishra et al., "Mapping the receptor binding regions of human chorionic gonadotropin (hCG)using disulfide peptides of its beta-subunit: possible involvement of the disulfide bonds Cys(9)-Cys(57) and Cys(23)-Cys(72) in receptor binding of the hormone", J PEPT RES, 58(1), 2001, pp. 17-26

Abstract

Human chorionic gonadotropin (hCG) is a heterodimeric glycoprotein hormoneessential for the establishment and maintenance of pregnancy, The alpha- and beta- subunits of hCG are highly cross-linked internally by disulfide bonds which seem to stabilize the tertiary structures required for the noncovalent association of the subunits to generate hormonal activity. The purpose of this study was to delineate the role of the disulfide bonds of hCG beta in receptor binding of the hormone. Six disulfide peptides incorporating each of the six disulfide bonds of hCG beta were synthesized and screened, along with their linear counterparts, for their ability to competitively inhibit the binding of [I-125] hCG to sheep ovarian corpora luteal LH/CG receptor. Disulfide peptide Cys (9-57) was found to be approximate to 4-fold more potent than the most active of its linear counterparts in inhibiting radiolabeled hCG from binding to its receptor. Similarly, disulfide peptide Cys (23-72) exhibited receptor binding inhibition activity, whereas the constituent linear peptides were found to be inactive. The results suggest the involvement of the disulfide bonds Cys(9)-Cys(57) and Cys(23)- Cys(72) of the beta -subunit of hCG in receptor binding of the hormone. This study is the first of its kind to use disulfide peptides rather than linear peptides to map the receptor binding regions of hCG.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 06:29:25