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Titolo:
METABOLIC EVOLUTION IN ALPHA-AMYLASES HORN DROSOPHILA-VIRILIS AND DROSOPHILA-REPLETA, 2 SPECIES WITH DIFFERENT ECOLOGICAL NICHES
Autore:
PRIGENT S; MATOUB M; ROULAND C; CARIOU ML;
Indirizzi:
CNRS,UPR 9034 F-91198 GIF SUR YVETTE FRANCE CNRS,UPR 9034 F-91198 GIF SUR YVETTE FRANCE UNIV PARIS 12,LAB ECOPHYSIOL INVERTEBRES F-94010 CRETEIL FRANCE
Titolo Testata:
Comparative biochemistry and physiology. B. Comparative biochemistry
fascicolo: 2, volume: 119, anno: 1998,
pagine: 407 - 412
SICI:
0305-0491(1998)119:2<407:MEIAHD>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADAPTIVE SIGNIFICANCE; FOOD COMPONENTS; MELANOGASTER; POLYMORPHISM; GENE; SUBGROUP; FREQUENCIES; SUBOBSCURA; ANANASSAE; VARIANTS;
Keywords:
DROSOPHILA VIRILIS; DROSOPHILA-REPLETA; ALPHA-AMYLASE; PURIFICATION; BIOCHEMICAL CHARACTERISTICS; KINETIC PARAMETERS; SUBSTRATE SPECIFICITY; ADAPTATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
S. Prigent et al., "METABOLIC EVOLUTION IN ALPHA-AMYLASES HORN DROSOPHILA-VIRILIS AND DROSOPHILA-REPLETA, 2 SPECIES WITH DIFFERENT ECOLOGICAL NICHES", Comparative biochemistry and physiology. B. Comparative biochemistry, 119(2), 1998, pp. 407-412

Abstract

alpha-Amylases from Drosophila virilis and D. repleta were partially purified by ion exchange chromatography. The two amylases share commoncharacteristics for pH and cations effects, although with slight differences. D. virilis has optimal activity at pH 6.6 and D. repleta at pH 7.2. Calcium, sodium, and potassium cations activate amylolytic activity in both species but Ba2+ has an activation effect in D. repleta only. In contrast, there are major differences in thermal stability andkinetics among amylases of the two species. D. virilis amylase is much more stable at high temperature and the optimal temperatures are very different between the two species, respectively, 45 degrees C and 30degrees C for D. virilis and D. repleta. alpha-Amylase activity usingdifferent substrates is greater on starch than on glycogen in both species and still higher on amylose for D. virilis, the nonfungus feederspecies. alpha-Amylase of D. repleta, the mycophagous species, has a better affinity to amylopectin and glycogen. Such differences in substrate specificity suggest adaptation to different resources in these species living in different habitats. Metabolic evolution seems to have occurred through a ''tradeoff'' between kinetic effectiveness and the nature of substrate, with a higher V-max on amylose for D. virilis anda lower K-m on glycogen for D. repleta. (C) 1998 Elsevier Science Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 22:25:54