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Titolo:
ALBUMIN HAWKES BAY - A LOW-LEVEL VARIANT CAUSED BY LOSS OF A SULFHYDRYL-GROUP AT POSITION-177
Autore:
BRENNAN SO; FELLOWES AP;
Indirizzi:
PATHOL SERV,CLIN BIOCHEM UNIT,MOLEC PATHOL LAB,POB 151 CHRISTCHURCH NEW ZEALAND
Titolo Testata:
Biochimica et biophysica acta
fascicolo: 1, volume: 1182, anno: 1993,
pagine: 46 - 50
SICI:
0006-3002(1993)1182:1<46:AHB-AL>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-SERUM-ALBUMIN; MUTATION; SITE;
Keywords:
SERUM ALBUMIN; LOW LEVEL VARIANT; AMINO ACID SUBSTITUTION; PROTEIN ELECTROPHORESIS, 2-DIMENSIONAL; DISULFIDE BRIDGE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
10
Recensione:
Indirizzi per estratti:
Citazione:
S.O. Brennan e A.P. Fellowes, "ALBUMIN HAWKES BAY - A LOW-LEVEL VARIANT CAUSED BY LOSS OF A SULFHYDRYL-GROUP AT POSITION-177", Biochimica et biophysica acta, 1182(1), 1993, pp. 46-50

Abstract

A slow migrating minor albumin component, representing 5% of total circulating albumin, was detected by routine serum protein electrophoresis and immunofixation. After treatment with 5 mM dithiothreitol the abnormal component was found to migrate normally suggesting the attachment of some component to the free thiol at position 34. However, purification and analysis by SDS-PAGE showed that the abnormal component hada slightly lower apparent molecular weight than normal albumin. Limited tryptic cleavage indicated the abnormal site to be in the N-terminal third of the molecule. HPLC analysis of tryptic peptides from this domain showed the presence of a new peptide of sequence Ala-Ala-Phe-Leu-Leu-Pro-Lys, indicating either a point mutation of 177 Cys --> Phe orthe deletion of residues 166-177. DNA sequencing of PCR-amplified DNAconfirmed the former Cys --> Phe substitution by indicating a point mutation of C to A at nucleotide position 5185. It appears that the aberrant electrophoretic mobility of the variant might be due to a gross conformational change associated with the formation of a new disulphide bond between Cys-168 and Cys-124.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 06:23:18