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Titolo:
Determination of the complete covalent structure of the major glycoform ofDQH sperm surface protein, a novel trypsin-resistant boar seminal plasma O-glycoprotein related to pB1 protein
Autore:
Bezouska, K; Sklenar, J; Novak, P; Halada, P; Havlicek, V; Kraus, M; Ticha, M; Jonakova, V;
Indirizzi:
Charles Univ, Fac Sci, Dept Biochem, CZ-12840 Prague 2, Czech Republic Charles Univ Prague Czech Republic 2 , CZ-12840 Prague 2, Czech Republic Acad Sci Czech Republ, Inst Microbiol, CZ-14220 Prague, Czech Republic Acad Sci Czech Republ Prague Czech Republic CZ-14220 gue, Czech Republic Acad Sci Czech Republ, Inst Mol Genet, CZ-16637 Prague 6, Czech Republic Acad Sci Czech Republ Prague Czech Republic 6 7 Prague 6, Czech Republic
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 7, volume: 8, anno: 1999,
pagine: 1551 - 1556
SICI:
0961-8368(199907)8:7<1551:DOTCCS>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; HEPARIN-BINDING; SPERMADHESINS; DOMAIN; AQN;
Keywords:
boar seminal plasma; DQH sperm surface protein; ESI-MS; fibronectin type II repeat; MALDI-MS; O-glycosylation; post-source decay MALDI-MS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Bezouska, K Charles Univ, Fac Sci, Dept Biochem, Hlavova 8, CZ-12840 Prague 2, Czech Republic Charles Univ Hlavova 8 Prague Czech Republic 2 Czech Republic
Citazione:
K. Bezouska et al., "Determination of the complete covalent structure of the major glycoform ofDQH sperm surface protein, a novel trypsin-resistant boar seminal plasma O-glycoprotein related to pB1 protein", PROTEIN SCI, 8(7), 1999, pp. 1551-1556

Abstract

The complete covalent structure of a novel boar DQH sperm surface protein resistant to many classical procedures of enzymatic fragmentation was determined. The relative molecular mass of the major form of this protein determined by ESI-MS and MALDI-MS was 13,065.2 +/- 1.0 and 13,065.1, respectively. However, additional peaks differing by 162 Da (i.e., minus hexose), 365 Da (i.e., minus hexose and N-acetylhexosamine), 146 Da (i.e., plus deoxyhexose), and 291 Da (i.e., plus sialic acid) indicated the heterogeneity due todifferences in glycosylation. The complete covalent structure of the protein was determined using automated Edman degradation, MALDI-MS, and post-source decay (PSD) MALDI-MS, and shown to consist of N-terminal O-glycosylatedpeptide followed by two fibronectin type II repeats. The carbohydrates areO-glycosidically linked to threonine 10, as confirmed by PSD MALDI-MS of the isolated N-terminal glycopeptide. Eight cysteine residues of the proteinform four disulfide bridges, the positions of which were assigned from MALDI-MS and Edman degradation data. We conclude that mass spectral techniquesprovide an indispensable tool for the detailed analysis of the covalent structure of proteins, especially those that are refractory to standard approaches of protein chemistry.

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Documento generato il 27/11/20 alle ore 02:15:56