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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2001

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Assignment of the complete disulphide bridge pattern in the human recombinant follitropin beta-chain.

Anno di pubblicazione: 2001

Autori: Amoresano A, Orrù S, Siciliano RA, De Luca E, Napoleoni R, Sirna A, Pucci P.

Affiliazioni autori: Centro Internazionale di Servizi di Spettrometria di Massa, CNR-Università di Napoli Federico II, Napoli, Italy Istituto di Scienze dell'Alimentazione del CNR, Avellino

Autori CNR:

  • ROSA ANNA SICILIANO

Abstract: The chemical assessment of the complete disulphide bridge pattern in the beta-chain of human recombinant follicotropin (betaFSH) was accomplished by integrating classical biochemical methodologies with mass spectrometric procedures. A proteolytic strategy consisting of a double digestion of native betaFSH using the broad-specificity protease subtilisin first, followed by trypsin, was employed. The resulting peptide mixture was directly analysed by FAB-MS, leading to the assignment of the first three disulphide bridges. The remaining S-S bridges were determined by HPLC fractionation of the proteolytic digest followed by ESMS analysis of the individual fractions. The pattern of cysteine couplings in betaFSH was determined as: Cys3-Cys5l, Cys17-Cys66, Cys20-Cys104, Cys28-Cys82, Cys32-Cys84 and Cys87-Cys94, confirming the arrangement inferred from the crystal structure of the homologous betaCG. A subset of the S-S bridge pattern comprising Cys3-Cys51, Cys28-Cys82 and Cys32-Cys84 constitutes a cysteine knot motif similar to that found in the growth factor superfamily

Pagine da: 961

Pagine a: 968

Rivista:

Biological chemistry de Gruyter.
Paese di pubblicazione: Germania
Lingua: inglese
ISSN: 1431-6730

Numero volume: 382

Strutture CNR:

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