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Titolo:
LIPIDS ARE COVALENTLY ATTACHED TO RIGID CORNEOCYTE PROTEIN ENVELOPES EXISTING PREDOMINANTLY AS BETA-SHEETS - A SOLID-STATE NUCLEAR-MAGNETIC-RESONANCE STUDY
Autore:
LAZO ND; MEINE JG; DOWNING DT;
Indirizzi:
UNIV IOWA,COLL MED,MED LABS 270 IOWA CITY IA 52242 UNIV IOWA,COLL MED,DEPT DERMATOL,MARSHALL RES LABS IOWA CITY IA 52242
Titolo Testata:
Journal of investigative dermatology
fascicolo: 2, volume: 105, anno: 1995,
pagine: 296 - 300
SICI:
0022-202X(1995)105:2<296:LACATR>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
KERATIN INTERMEDIATE FILAMENTS; STRATUM-CORNEUM; CARBON RESONANCES; SOFT-TISSUES; C-13 NMR; RESOLUTION; EPIDERMIS; LORICRIN; DYNAMICS; COLLAGEN;
Keywords:
EPIDERMIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
N.D. Lazo et al., "LIPIDS ARE COVALENTLY ATTACHED TO RIGID CORNEOCYTE PROTEIN ENVELOPES EXISTING PREDOMINANTLY AS BETA-SHEETS - A SOLID-STATE NUCLEAR-MAGNETIC-RESONANCE STUDY", Journal of investigative dermatology, 105(2), 1995, pp. 296-300

Abstract

C-13 solid-state nuclear magnetic resonance at natural abundance was used to study isolated corneocyte envelopes from porcine stratum corneum. The presence of lipids covalently attached to the protein envelopes was detected by chemical shifts of methylene and methyl groups of the bound lipids. The corneocyte protein envelopes are rigid, as suggested by efficient H-1 to C-13 cross polarization and C-13 spin-lattice relaxation studies. The chemical shift of the carbonyl carbons of the protein envelopes supports the prediction that the chemically bound lipid envelope is attached to proteins arranged predominantly in the beta-sheet conformation, allowing a dense palisade of ceramide molecules to form a water-impermeable external sheath.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 14:19:18