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Titolo:
CHARACTERIZATION OF O-GLYCOSYLATED PRECURSORS OF INSULIN-LIKE GROWTH-FACTOR-II BY MATRIX-ASSISTED LASER-DESORPTION IONIZATION MASS-SPECTROMETRY
Autore:
JESPERSEN S; KOEDAM JA; HOOGERBRUGGE CM; TJADEN UR; VANDERGREEF J; VANDENBRANDE JL;
Indirizzi:
TNO,CTR STRUCT ELUDICAT & INSTRUMENTAL ANAL,POB 360 NL-3700 AJ ZEIST NETHERLANDS LEIDEN UNIV,CTR BIOPHARMACEUT SCI,DIV ANALYT CHEM NL-2300 RA LEIDEN NETHERLANDS WILHELMINA CHILDRENS HOSP,DEPT ENDOCRINOL NL-3501 CA UTRECHT NETHERLANDS
Titolo Testata:
Journal of mass spectrometry.
fascicolo: 8, volume: 31, anno: 1996,
pagine: 893 - 900
SICI:
1076-5174(1996)31:8<893:COOPOI>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
IGF-II; TUMOR HYPOGLYCEMIA; PROTEINS; PEPTIDE; IDENTIFICATION; BIOPOLYMERS; SEQUENCE; VARIANT; FORM;
Keywords:
MATRIX-ASSISTED LASER DESORPTION IONIZATION; PRECURSOR INSULIN-LIKE GROWTH FACTOR II; O-GLYCOSYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
27
Recensione:
Indirizzi per estratti:
Citazione:
S. Jespersen et al., "CHARACTERIZATION OF O-GLYCOSYLATED PRECURSORS OF INSULIN-LIKE GROWTH-FACTOR-II BY MATRIX-ASSISTED LASER-DESORPTION IONIZATION MASS-SPECTROMETRY", Journal of mass spectrometry., 31(8), 1996, pp. 893-900

Abstract

High molecular weight precursors of insulin-like growth factor II (IGF-LI) were isolated from Cohn fraction IV of human plasma by ultrafiltration, affinity chromatography and reversed-phase high-performance liquid chromatography. Molecular weight determination by matrix-assistedlaser desorption/ionization mass spectrometry (MALDI-MS) of two high molecular weight IGF-II preparations revealed heterogeneous glycosylation. A combination of enzymatic degradation and MALDI-MS were applied for further structural characterization of the glycosylated precursorsof IGF-II. The first step was molecular weight determination of intact high molecular weight IGF-IIs prior to and after treatment with neuraminidase and O-glycosidase. This, together with a comparison of molecular weight information available from the cDNA, revealed that both high molecular weight IGF-II species contain an identical C-terminal extension of 20 residues but different degrees of glycosylation. Second, comparative Endo Glu-C digestion of the preparations prior to and after enzymatic release of carbohydrates and subsequent remeasurement of the molecular weight by MALDI-MS confirmed the primary structure of precursor IGF-II1-87. The O-linked carbohydrates were found to be associated with the C-terminal extension and the heterogeneity was identifiedas varied sialylated forms of one and two HexNAc-Hex groups.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 20:05:21