Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Evaluation of peptide electropherograms by multivariate mathematical-statistical methods I. Principal component analysis
Autore:
Miksik, I; Eckhardt, A; Cserhati, T; Forgacs, E; Zicha, J; Deyl, Z;
Indirizzi:
Acad Sci Czech Republ, Inst Physiol, CR-14220 Prague, Czech Republic Acad Sci Czech Republ Prague Czech Republic CR-14220 gue, Czech Republic Hungarian Acad Sci, Budapest, Hungary Hungarian Acad Sci Budapest Hungary ngarian Acad Sci, Budapest, Hungary Dept Analyt Chem, Inst Chem Technol, Prague, Czech Republic Dept Analyt Chem Prague Czech Republic Technol, Prague, Czech Republic Charles Univ, Sch Med 2, Dept Physiol, Prague, Czech Republic Charles Univ Prague Czech Republic Dept Physiol, Prague, Czech Republic Ctr Expt Cardiovasc Res, Prague, Czech Republic Ctr Expt Cardiovasc Res Prague Czech Republic s, Prague, Czech Republic
Titolo Testata:
JOURNAL OF CHROMATOGRAPHY A
fascicolo: 1, volume: 921, anno: 2001,
pagine: 81 - 91
Fonte:
ISI
Lingua:
ENG
Soggetto:
CAPILLARY-ELECTROPHORESIS; COLLAGEN; LIPOPHILICITY; GLYCATION;
Keywords:
principal component analysis; statistical analysis; peptides; collagens;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
18
Recensione:
Indirizzi per estratti:
Indirizzo: Miksik, I Acad Sci Czech Republ, Inst Physiol, Videnska 1083,4-KRC, CR-14220 Prague,Czech Republic Acad Sci Czech Republ Videnska 1083,4-KRC Prague Czech Republic CR-14220
Citazione:
I. Miksik et al., "Evaluation of peptide electropherograms by multivariate mathematical-statistical methods I. Principal component analysis", J CHROMAT A, 921(1), 2001, pp. 81-91

Abstract

Depository effects in slowly metabolised proteins, typically glycation or the estimation of products arising from the reaction of unsaturated long-chain-fatty acid metabolites (possessing aldehydic groups) are very difficultto assess owing to their extremely low concentration in the protein matrix. In order to reveal such alterations we applied deep enzymatic fragmentation resulting in a set of small peptides, which, if modified, are likely to change their electrophoretic properties and can be visualised on the resulting profile. Peptide maps of collagen (a mixture of collagen types I and III digested by bacterial collagenase) were applied as the model protein structure for detecting the nonenzymatic posttranslational changes originating during various physiological conditions like high fructose diet and hypertriglyceridemic state. Capillary electrophoresis in acidic media (sodium phosphate buffer, pH 2.5) was used as the separation method capable of (partial) separation of over 60 peptide peaks. Two to 13 changes were revealed in the profiles obtained reflecting the physiological conditions of the animalstested. Combination of peptide profiling with subsequent t-test evaluationof individual peak areas and principal component analysis based on cumulative peak areas of individual sections of the electropherograms allowed to determine in which section (part) of the electropherogram the physiological state indicating changes occurred. Simultaneously it was possible to revealthe qualitative differences between the four physiological regimes investigated (i.e., which regime affects the collagen molecules most and which affects them least). The approach can be used as guidance for targeted preseparation of the very complex peptide mixture. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 12:15:00