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Titolo:
IDENTIFICATION OF N-LINKED GLYCOSYLATION SITES IN HUMAN TESTIS ANGIOTENSIN-CONVERTING ENZYME AND EXPRESSION OF AN ACTIVE DEGLYCOSYLATED FORMS
Autore:
YU XC; STURROCK ED; WU ZC; BIEMANN K; EHLERS MRW; RIORDAN JF;
Indirizzi:
HARVARD UNIV,SCH MED,CTR BIOCHEM & BIOPHYS SCI & MED,250 LONGWOOD AVEBOSTON MA 02115 HARVARD UNIV,SCH MED,CTR BIOCHEM & BIOPHYS SCI & MED BOSTON MA 02115 MIT,DEPT CHEM CAMBRIDGE MA 02139 UNIV CAPE TOWN,SCH MED,DEPT BIOCHEM MED ZA-7925 CAPE TOWN SOUTH AFRICA
Titolo Testata:
The Journal of biological chemistry
fascicolo: 6, volume: 272, anno: 1997,
pagine: 3511 - 3519
SICI:
0021-9258(1997)272:6<3511:IONGSI>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLYCANS; SECRETION; SEQUENCE; BINDING; CELLS; CHAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
X.C. Yu et al., "IDENTIFICATION OF N-LINKED GLYCOSYLATION SITES IN HUMAN TESTIS ANGIOTENSIN-CONVERTING ENZYME AND EXPRESSION OF AN ACTIVE DEGLYCOSYLATED FORMS", The Journal of biological chemistry, 272(6), 1997, pp. 3511-3519

Abstract

The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion. Two of the seven potential N-linked glycosylation sites, Asn(90)and Asn(109), were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and withendoproteinase Asp-N, The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans intACE to be mostly of the biantennary, fucosylated complex type, This structural information was used to demonstrate that three other sites,Asn(155), Asn(337), and Asn(586) are partially glycosylated, whereas Asn(72) appears to be fully glycosylated, The only potential site thatwas not modified is Asn(620), Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn. Only one of these glycosylation sites had a counterpart in tACE, Comparison of the two proteins reveals a pattern in which amino-terminal N-linked sites are preferred. The functional significance of glycosylation was examined with a tACE mutant lacking the O-glycan-rich first amino-terminal 36 residues and truncated at Ser(625). When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.

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Documento generato il 25/09/20 alle ore 09:16:31