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Titolo:
PURIFICATION AND CHEMICAL CHARACTERIZATION OF BETA-TRACE PROTEIN FROMHUMAN CEREBROSPINAL-FLUID - ITS IDENTIFICATION AS PROSTAGLANDIN-D SYNTHASE
Autore:
HOFFMANN A; CONRADT HS; GROSS G; NIMTZ M; LOTTSPEICH F; WURSTER U;
Indirizzi:
GBF GESELL BIOTECHNOL FORSCH,DEPT CELL BIOL & GENET,MASCHERODER WEG 7W-3300 BRAUNSCHWEIG GERMANY GBF GESELL BIOTECHNOL FORSCH,DEPT CELL BIOL & GENET,MASCHERODER WEG 7W-3300 BRAUNSCHWEIG GERMANY HANNOVER MED SCH,DEPT NEUROL,CSF LAB W-3000 HANNOVER 61 GERMANY MAX PLANCK INST BIOCHEM W-8033 MARTINSRIED GERMANY
Titolo Testata:
Journal of neurochemistry
fascicolo: 2, volume: 61, anno: 1993,
pagine: 451 - 456
SICI:
0022-3042(1993)61:2<451:PACCOB>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
HAMSTER OVARY CELLS; SENSITIVE METHOD; ANTIGEN; CHAINS;
Keywords:
CSF; HUMAN BETA-TRACE PROTEIN; HUMAN PROSTAGLANDIN-D SYNTHASE; PROTEIN PRIMARY STRUCTURE; N-GLYCOSYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
19
Recensione:
Indirizzi per estratti:
Citazione:
A. Hoffmann et al., "PURIFICATION AND CHEMICAL CHARACTERIZATION OF BETA-TRACE PROTEIN FROMHUMAN CEREBROSPINAL-FLUID - ITS IDENTIFICATION AS PROSTAGLANDIN-D SYNTHASE", Journal of neurochemistry, 61(2), 1993, pp. 451-456

Abstract

Beta-Trace protein from pooled human CSF was purified to homogeneity. An apparent molecular mass of 23-29 kDa was determined for the polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amino-terminal sequencing of the polypeptide yielded the unique amino acid sequence APEAQVSVQPNFQQDKFLGRWFSA24. Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H-2 D-isomerase; (5Z, ha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2]. A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide. The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate. Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha2-3- and/or alpha2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine. Agalacto structures as well as those with a peripheral fucose are also present.

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Documento generato il 29/03/20 alle ore 11:19:08