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Titolo:
Purification and characterization of proline-rich proteins from developingembryos of the camel tick Hyalomma dromedarii
Autore:
Fahmy, AS; Ghany, SSA; Mohamed, SA; Mohamed, MA; Mohamed, TM;
Indirizzi:
Natl Res Ctr, Dept Biol Mol, Cairo, Egypt Natl Res Ctr Cairo EgyptNatl Res Ctr, Dept Biol Mol, Cairo, Egypt
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
fascicolo: 3, volume: 121, anno: 1998,
pagine: 279 - 290
SICI:
0305-0491(199811)121:3<279:PACOPP>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN PAROTID-SALIVA; STRUCTURAL PROTEIN; LOCUSTA-MIGRATORIA; CALCIUM; CUTICLE; BINDING; PHOSPHOPROTEIN; SPERMATOPHORE; SEQUENCE;
Keywords:
embryogenesis; characterization; Hyalomma dromedarii; proline-rich proteins; purification;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Fahmy, AS Natl Res Ctr, Dept Biol Mol, Cairo, Egypt Natl Res Ctr Cairo Egypt Res Ctr, Dept Biol Mol, Cairo, Egypt
Citazione:
A.S. Fahmy et al., "Purification and characterization of proline-rich proteins from developingembryos of the camel tick Hyalomma dromedarii", COMP BIOC B, 121(3), 1998, pp. 279-290

Abstract

The levels of acidic and basic proline-rich proteins in the camel tick Hyalomma dromedarii has been followed throughout embryogenesis, The developmental profiles of proline content in the crude protein fractions showed significant changes which would have to be of greater physiological consequences. During purification of FIIa to homogeneity the ion exchange chromatography step lead to separation of nine peaks where five of them were rich in proline. Gel filtration of FIIa peak 9 on Sephadex G-ZOO separated two forms (A and B) with proline/protein% of 23.75 and 2.35%, respectively. Peak A wasproved to be pure by SDS-PAGE. FIb and FIIb were separated into four and five peaks by gel filtration on Sephadex G-200, Peaks 4 of FIb and FIIb wereproved to be pure by SDS-PAGE with proline/protein% of 40.26 and 12.60%, respectively. FIIa, FIb and FIIb had different molecular weights (104000-50000, 24000-23000 and 16000-17000 for the native and denatured proteins, respectively), amino acid composition and carbohydrate/protein%. The purified FIIa and FIIb had the ability to bind calcium and their maximum binding are exhibited at pH's 3.5 and 6.5, respectively at 37 degrees C. The effect of bivalent metals and proteolytic digestion on the binding of calcium to proline-rich proteins was studied, (C) 1998 Elsevier Science Inc. All rights reserved.

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Documento generato il 19/09/20 alle ore 08:36:02