Data/hora: 10/06/2024 17:04:38

Provedor de dados: | 80
País: | Brazil
Título: | Hymenoptera venom review focusing on Apis mellifera
Autores: | Lima,P. R. de; Brochetto-Braga,M. R.
Data: | 2003-01-01
Ano: | 2003
Palavras-chave: | Hymenoptera; Venom; Enzymes; Peptides.
Resumo: | Hymenoptera venoms are complex mixtures containing simple organic molecules, proteins, peptides, and other bioactive elements. Several of these components have been isolated and characterized, and their primary structures determined by biochemical techniques. These compounds are responsible for many toxic or allergic reactions in different organisms, such as local pain, inflammation, itching, irritation, and moderate or severe allergic reactions. The most extensively characterized Hymenoptera venoms are bee venoms, mainly from the Apis genus and also from social wasps and ant species. However, there is little information about other Hymenoptera groups. The Apis venom presents high molecular weight molecules - enzymes with a molecular weight higher than 10.0 kDa - and peptides. The best studied enzymes are phospholipase A2, responsible for cleaving the membrane phospholipids, hyaluronidase, which degrades the matrix component hyaluronic acid into non-viscous segments and acid phosphatase acting on organic phosphates. The main peptide compounds of bee venom are lytic peptide melittin, apamin (neurotoxic), and mastocyte degranulating peptide (MCD).
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992003000200002
Editor: | Centro de Estudos de Venenos e Animais Peçonhentos
Relação: | 10.1590/S1678-91992003000200002
Formato: | text/html
Fonte: | Journal of Venomous Animals and Toxins including Tropical Diseases  v.9 n.2 2003
Fonte: | info:eu-repo/semantics/openAccess