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| Bordon,Karla C F; Wiezel,Gisele A.; Amorim,Fernanda G.; Arantes,Eliane C.. |
| AbstractHyaluronidases are enzymes that mainly degrade hyaluronan, the major glycosaminoglycan of the interstitial matrix. They are involved in several pathological and physiological activities including fertilization, wound healing, embryogenesis, angiogenesis, diffusion of toxins and drugs, metastasis, pneumonia, sepsis, bacteremia, meningitis, inflammation and allergy, among others. Hyaluronidases are widely distributed in nature and the enzymes from mammalian spermatozoa, lysosomes and animal venoms belong to the subclass EC 3.2.1.35. To date, only five three-dimensional structures for arthropod venom hyaluronidases (Apis mellifera and Vespula vulgaris) were determined. Additionally, there are four molecular models for hyaluronidases fromMesobuthus... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Hyaluronidase; Scorpion; Spider; Caterpillar; Hymenoptera; Insects; Cloning; Heterologous expression; PEGylation; Biotechnological applications. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100214 |
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| Bordon,Karla C. F.; Wiezel,Gisele A.; Cabral,Hamilton; Arantes,Eliane C.. |
| BackgroundCrotalus durissus terrificus venom (CdtV) is one of the most studied snake venoms in Brazil. Despite presenting several well known proteins, its L-amino acid oxidase (LAAO) has not been studied previously. This study aimed to isolate, characterize and evaluate the enzyme stability of bordonein-L, an LAAO from CdtV.Methods The enzyme was isolated through cation exchange, gel filtration and affinity chromatography, followed by a reversed-phase fast protein liquid chromatography to confirm its purity. Subsequently, its N-terminal amino acid sequence was determined by Edman degradation. The enzyme activity and stability were evaluated by a microplate colorimetric assay and the molecular mass was estimated by SDS-PAGE using periodic acid-Schiff... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Crotalus durissus terrificus; L-amino acid oxidase; Rattlesnake; Enzyme activity; Enzyme stability; Chromatography; Snake venom; Yellow venom; Stabilization. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100335 |
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