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Titolo:
Differences in midgut serine proteinases from larvae cf the bruchid beetles Callosobruchus maculatus and Zabrotes subfasciatus
Autore:
Silva, CP; Terra, WR; Lima, RM;
Indirizzi:
Univ Estadual Norte Fluminense, Ctr Biociencias & Biotecnol, Lab Quim & Funcao Prot & Peptideos, BR-28015620 Campos Dos Goytacazes, Brazil Univ Estadual Norte Fluminense Campos Dos Goytacazes Brazil BR-28015620 BC Univ Sao Paulo, Inst Quim, Dept Bioquim, BR-05599970 Sao Paulo, Brazil Univ Sao Paulo Sao Paulo Brazil BR-05599970 BC05599970 Sao Paulo, Brazil
Titolo Testata:
ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY
fascicolo: 1, volume: 47, anno: 2001,
pagine: 18 - 28
SICI:
0739-4462(200105)47:1<18:DIMSPF>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
OBTECTUS SAY COLEOPTERA; POSTERIOR MIDGUT; ALPHA-AMYLASES; BEAN WEEVIL; GUT; INHIBITOR; INSECTS; E-64;
Keywords:
bruchidae; proteinases; insect digestion; seed weevil;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Silva, CP Univ Estadual Norte Fluminense, Ctr Biociencias & Biotecnol, LabQuim & Funcao Prot & Peptideos, BR-28015620 Campos Dos Goytacazes, Brazil Univ Estadual Norte Fluminense Campos Dos Goytacazes Brazil BR-28015620 BC
Citazione:
C.P. Silva et al., "Differences in midgut serine proteinases from larvae cf the bruchid beetles Callosobruchus maculatus and Zabrotes subfasciatus", ARCH INS B, 47(1), 2001, pp. 18-28

Abstract

Proteinase activities in the larval midguts of the bruchids Callosobruchusmaculatus and Zabrotes subfasciatus were investigated. Both midgut homogenates showed a slightly acidic to neutral pH optima for the hydrolysis of fluorogenic substrates, Proteolysis of epsilon -aminocaproil-Leu-Cys(SBzl)-MCA was totally inhibited by the cysteine proteinase inhibitors E-64 and leupeptin, and was activated by 1.5 mM DTT in both insects, while hydrolysis ofthe substrate Z-ArgArg-MCA was inhibited by aprotinin and E-64, which suggests that it is being hydrolysed by serine and cysteine proteinases. Gel assays showed that the proteolytic activity in larval midgut of C. maculatus was due to five major cysteine proteinases. However, based on the pattern of E-64 and aprotinin inhibition, proteolytic activity in larval midgut of Z. subfasciatus was not due only to cysteine proteinases, Fractionation of the larval midgut homogenates of both bruchids through ion-exchange chromatography (DEAE-Sepharose) revealed two peaks of activity against Z-ArgArg-MCAfor both bruchid species. The fractions from C. maculatus have characteristics of cysteine proteinases, while Z. subfasciatus has one non-retained peak of activity containing cysteine proteinases and another eluted in a gradient of 250-350 mM NaCl. The proteolytic activity of the retained peak is higher at pH 8.8 than at pH 6.0 and corresponds with a single peak that is active against N-p-tosyl-GlyGlyArg-MCA, and sensitive to 250 muM aprotinin (90% inhibition). The peak contains a serine proteinase which hydrolyzes alpha -amylase inhibitor 1 from the common bean (Phaseolus vulgaris). (C) 2001Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 10:14:03