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Titolo:
Investigation of frozen protease-catalyzed peptide synthesis systems - a differential scanning calorimetry and electron microscopy approach
Autore:
Haensler, M; Maedler, B; Richter, W; Volke, F;
Indirizzi:
Univ Leipzig, Fac Biosci Pharm & Psychol, Inst Biochem, D-04103 Leipzig, Germany Univ Leipzig Leipzig Germany D-04103 t Biochem, D-04103 Leipzig, Germany Univ Leipzig, Fac Phys & Geosci, Inst Expt Phys 1, D-04103 Leipzig, Germany Univ Leipzig Leipzig Germany D-04103 pt Phys 1, D-04103 Leipzig, Germany IBMT, Faunhofer Inst Biomed Engn, D-66386 St Ingbert, Germany IBMT St Ingbert Germany D-66386 Biomed Engn, D-66386 St Ingbert, Germany
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 1-3, volume: 9, anno: 2000,
pagine: 91 - 95
SICI:
1381-1177(20000320)9:1-3<91:IOFPPS>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
AQUEOUS SYSTEMS; AMINO-ACIDS; CHYMOTRYPSIN;
Keywords:
differential scanning calorimetry; electron microscopy; frozen aqueous system; peptide synthesis; protease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
11
Recensione:
Indirizzi per estratti:
Indirizzo: Haensler, M Univ Leipzig, Fac Biosci Pharm & Psychol, Inst Biochem, Talstr33, D-04103Leipzig, Germany Univ Leipzig Talstr 33 Leipzig Germany D-04103 ipzig, Germany
Citazione:
M. Haensler et al., "Investigation of frozen protease-catalyzed peptide synthesis systems - a differential scanning calorimetry and electron microscopy approach", J MOL CAT B, 9(1-3), 2000, pp. 91-95

Abstract

The internal structure of a protease-catalyzed frozen aqueous peptide synthesis system was studied by freeze-fracture electron microscopy. Distinct lense-like liquid microinclusions differing in size from 0.25 to 1.7 mu m were observed. Differential scanning calorimetry was used to determine the amount of unfrozen water per molecule of peptide reactant. Comparison of the results with data obtained previously by examination of the same peptide synthesis system using H-1 NMR relaxation time technique showed that DSC is the more reliable method for this special purpose. Furthermore, the amount of unfrozen water in a frozen alpha-chymotrypsin solution determined by magic angle spinning NMR in previous investigations was confirmed by the calorimetric method. (C) 2000 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 18/01/21 alle ore 16:23:30