Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
CLONING AND SEQUENCE-ANALYSIS OF A CDNA CLONE CODING FOR THE MOUSE G(M2) ACTIVATOR PROTEIN
Autore:
BELLACHIOMA G; STIRLING JL; ORLACCHIO A; BECCARI T;
Indirizzi:
UNIV PERUGIA,DIPARTIMENTO MED SPERIMENTALE & SCI BIOCHIM,VIA GIOCHETTO,CP 37 SUCC 3 I-06126 PERUGIA ITALY KINGS COLL LONDON,DIV LIFE SCI LONDON W8 7AH ENGLAND
Titolo Testata:
Biochemical journal
, volume: 294, anno: 1993,
parte:, 1
pagine: 227 - 230
SICI:
0264-6021(1993)294:<227:CASOAC>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
GM2 ACTIVATOR; GANGLIOSIDE GM2; BETA-HEXOSAMINIDASE; SECONDARY-STRUCTURE; AB-VARIANT; GENE; CHROMOSOME-5; DEGRADATION; SUBUNIT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
22
Recensione:
Indirizzi per estratti:
Citazione:
G. Bellachioma et al., "CLONING AND SEQUENCE-ANALYSIS OF A CDNA CLONE CODING FOR THE MOUSE G(M2) ACTIVATOR PROTEIN", Biochemical journal, 294, 1993, pp. 227-230

Abstract

A cDNA (1.1 kb) containing the complete coding sequence for the mouseG(M2) activator protein was isolated from a mouse macrophage library using a cDNA for the human protein as a probe. There was a single ATG located 12 bp from the 5' end of the cDNA clone followed by an open reading frame of 579 bp. Northern blot analysis of mouse macrophage RNA showed that there was a single band with a mobility corresponding to asize of 2.3 kb. We deduce from this that the mouse mRNA, in common with the mRNA for the human G(M2) activator protein, has a long 3' untranslated sequence of approx. 1.7 kb. Alignment of the mouse and human deduced amino acid sequences showed 68% identity overall and 75% identity for the sequence on the C-terminal side of the first 31 residues, which in the human G(M2) activator protein contains the signal peptide. Hydropathicity plots showed great similarity between the mouse and human sequences even in regions of low sequence similarity. There is a single N-glycosylation site in the mouse G(M2) activator protein sequence (Asn151-Phe-Thr) which differs in its location from the single sitereported in the human G(M2) activator protein sequence (Asn63-Val-Thr).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 15:16:40