Isolation and partial characterization of a protease with kallikrein-like activity from the egg-nests of hylesia metabus (crammer 1775) (lepidoptera: saturnidae), preliminary communication
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| Format: | Artículo científico |
| Language: | en |
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Instituto Politécnico Nacional
2002
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| _version_ | 1876447599901278208 |
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| author | Ulf Lundberg |
| author_facet | Ulf Lundberg |
| contents | Isolation and partial characterization of a protease with kallikrein-like activity from the egg-nests of hylesia metabus (crammer 1775) (lepidoptera: saturnidae), preliminary communication Ulf Lundberg Frances Osborn Zoila Carvajal Amparo Gil Carmen Luisa Arocha Piñango Ingeniería protease kallikrein Hylesia metabus Hylesia metabus is a species of moth, distributed principally in North Eastern Venezuela.Adult females use their abdominal hairs to cover and protect the eggs from predators andparasites. These hairs have urticating properties, causing a severe dermatitis in humans,whose symptoms worsen using soap and are alleviated by slightly acid substances e.g.vinegar. The hairs from male moths however do not produce any symptoms. In thepresent study we have isolated and partially characterized a protease with kallikrein-likeactivity from the female abdominal hairs of this species. Egg-nests (consisting mainly offemale abdominal hairs) were collected from the twigs of mangrove-trees in affected areasafter hatching. The proteic substances were extracted into Tris -buffered saline solution atpH 8.5, centrifuged, and chromatographed by size-exclusion chromatography (SephadexG-75). Biological activity in the peaks was determined by amidolytic activity in thechromogenic substrates S-2288 (Broad Spectrum Serine Protease Substrate) and S-2302(Kallikrein substrate). The eluates showing biological activity were concentrated byultrafiltration and used for further analyses. The specificity in chromogenic substratesshowed a preference for the kallikrein substrate S-2302 followed by the broad-spectrumserine protease substrate S-2288. In addition the enzyme showed a pH optimum at pH 9,with no activity below pH 5. Thus the results of the present study support the hypothesisthat this substance may be of importance in the lesions observed in individuals exposed toadult females or the egg-nests. 2002 artículo científico 1665-0654 https://www.redalyc.org/articulo.oa?id=61412205 en http://www.redalyc.org/revista.oa?id=614 Científica application/pdf Instituto Politécnico Nacional Científica (México) Num.2 Vol.12 |
| format | Artículo científico |
| id | redalyc_61412205 |
| institution | Redalyc |
| language | en |
| publishDate | 2002 |
| publisher | Instituto Politécnico Nacional |
| spellingShingle | Isolation and partial characterization of a protease with kallikrein-like activity from the egg-nests of hylesia metabus (crammer 1775) (lepidoptera: saturnidae), preliminary communication Ulf Lundberg Ingeniería protease kallikrein Hylesia metabus Isolation and partial characterization of a protease with kallikrein-like activity from the egg-nests of hylesia metabus (crammer 1775) (lepidoptera: saturnidae), preliminary communication Ulf Lundberg Frances Osborn Zoila Carvajal Amparo Gil Carmen Luisa Arocha Piñango Ingeniería protease kallikrein Hylesia metabus Hylesia metabus is a species of moth, distributed principally in North Eastern Venezuela.Adult females use their abdominal hairs to cover and protect the eggs from predators andparasites. These hairs have urticating properties, causing a severe dermatitis in humans,whose symptoms worsen using soap and are alleviated by slightly acid substances e.g.vinegar. The hairs from male moths however do not produce any symptoms. In thepresent study we have isolated and partially characterized a protease with kallikrein-likeactivity from the female abdominal hairs of this species. Egg-nests (consisting mainly offemale abdominal hairs) were collected from the twigs of mangrove-trees in affected areasafter hatching. The proteic substances were extracted into Tris -buffered saline solution atpH 8.5, centrifuged, and chromatographed by size-exclusion chromatography (SephadexG-75). Biological activity in the peaks was determined by amidolytic activity in thechromogenic substrates S-2288 (Broad Spectrum Serine Protease Substrate) and S-2302(Kallikrein substrate). The eluates showing biological activity were concentrated byultrafiltration and used for further analyses. The specificity in chromogenic substratesshowed a preference for the kallikrein substrate S-2302 followed by the broad-spectrumserine protease substrate S-2288. In addition the enzyme showed a pH optimum at pH 9,with no activity below pH 5. Thus the results of the present study support the hypothesisthat this substance may be of importance in the lesions observed in individuals exposed toadult females or the egg-nests. 2002 artículo científico 1665-0654 https://www.redalyc.org/articulo.oa?id=61412205 en http://www.redalyc.org/revista.oa?id=614 Científica application/pdf Instituto Politécnico Nacional Científica (México) Num.2 Vol.12 |
| title | Isolation and partial characterization of a protease with kallikrein-like activity from the egg-nests of hylesia metabus (crammer 1775) (lepidoptera: saturnidae), preliminary communication |
| topic | Ingeniería protease kallikrein Hylesia metabus |
| url | https://www.redalyc.org/articulo.oa?id=61412205 |