Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venom

Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venom

Some properties of a Africanized honeybee venom proteases were determined by enzymatic assays in solution, electrophoresis in SDS-PAGE, and gel filtration. Bee venom extracts were obtained by reservoir disruption, selective dialysis (cut off 12 kDa) to eliminate small components, such as the protease inhibitor present in the venom, and then fractionation of the dialyzed extract by gel filtration on a Sephadex G-100 column. The optimal conditions for the caseinolytic assays were pH 9.5, 2-hour digestion at 37 °C, and 1% casein concentration. The proteolytic activity was also determined by electrophoresis in SDS-PAGE with co-polymerized gelatin with three major bands of 66.0, 41.6, and 25.1 kDa. A principal serine-protease-like mechanism was revealed in the enriched fraction of proteolytic activity.

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Main Authors: LIMA,P. R. M. DE, BROCHETTO-BRAGA,M. R., CHAUD-NETTO,J.
Format: Digital revista
Language:English
Published: Centro de Estudos de Venenos e Animais Peçonhentos - CEVAP, Universidade Estadual Paulista - UNESP 2000
Online Access:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79302000000100004
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spelling oai:scielo:S0104-793020000001000042000-02-25Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venomLIMA,P. R. M. DEBROCHETTO-BRAGA,M. R.CHAUD-NETTO,J. venom africanized bee Apis mellifera proteolytic activity gel filtration chromatography Some properties of a Africanized honeybee venom proteases were determined by enzymatic assays in solution, electrophoresis in SDS-PAGE, and gel filtration. Bee venom extracts were obtained by reservoir disruption, selective dialysis (cut off 12 kDa) to eliminate small components, such as the protease inhibitor present in the venom, and then fractionation of the dialyzed extract by gel filtration on a Sephadex G-100 column. The optimal conditions for the caseinolytic assays were pH 9.5, 2-hour digestion at 37 °C, and 1% casein concentration. The proteolytic activity was also determined by electrophoresis in SDS-PAGE with co-polymerized gelatin with three major bands of 66.0, 41.6, and 25.1 kDa. A principal serine-protease-like mechanism was revealed in the enriched fraction of proteolytic activity.info:eu-repo/semantics/openAccessCentro de Estudos de Venenos e Animais Peçonhentos - CEVAP, Universidade Estadual Paulista - UNESPJournal of Venomous Animals and Toxins v.6 n.1 20002000-01-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79302000000100004en10.1590/S0104-79302000000100004
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country Brasil
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libraryname SciELO
language English
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author LIMA,P. R. M. DE
BROCHETTO-BRAGA,M. R.
CHAUD-NETTO,J.
spellingShingle LIMA,P. R. M. DE
BROCHETTO-BRAGA,M. R.
CHAUD-NETTO,J.
Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venom
author_facet LIMA,P. R. M. DE
BROCHETTO-BRAGA,M. R.
CHAUD-NETTO,J.
author_sort LIMA,P. R. M. DE
title Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venom
title_short Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venom
title_full Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venom
title_fullStr Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venom
title_full_unstemmed Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venom
title_sort proteolytic activity of africanized honeybee (apis mellifera: hymenoptera, apidae) venom
description Some properties of a Africanized honeybee venom proteases were determined by enzymatic assays in solution, electrophoresis in SDS-PAGE, and gel filtration. Bee venom extracts were obtained by reservoir disruption, selective dialysis (cut off 12 kDa) to eliminate small components, such as the protease inhibitor present in the venom, and then fractionation of the dialyzed extract by gel filtration on a Sephadex G-100 column. The optimal conditions for the caseinolytic assays were pH 9.5, 2-hour digestion at 37 °C, and 1% casein concentration. The proteolytic activity was also determined by electrophoresis in SDS-PAGE with co-polymerized gelatin with three major bands of 66.0, 41.6, and 25.1 kDa. A principal serine-protease-like mechanism was revealed in the enriched fraction of proteolytic activity.
publisher Centro de Estudos de Venenos e Animais Peçonhentos - CEVAP, Universidade Estadual Paulista - UNESP
publishDate 2000
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79302000000100004
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AT chaudnettoj proteolyticactivityofafricanizedhoneybeeapismelliferahymenopteraapidaevenom
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