Characterization of a proteolytic enzyme from Lachesis muta venom (Serpentes: Viperidae)
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| Định dạng: | artículo original |
| Trạng thái: | Versión publicada |
| Ngày xuất bản: | 1992 |
| Miêu tả: | A proteolytic enzyme from L. muta stenophrys was isolated by gel filtration on Bio Gel P-l00 followed by FPLC on MONO S column. The enzyme exhibited proteolytic activity toward casein,hemoglobin and fibrinogen with a pH optimum around 10. The activity was inhibited by BDTA while trypsin inhibitors were not inhibitory. It is a glycoprotein, Mr 14 kDa with a high content of Asp,Glu,and Leu residues and a low content of Cys and Trp. The protease is devoid of myotoxic, hemorrhagic, esterolytic and amidolytic activities. It Iyses the alfa and beta chains of human fibrinogen and releases kinin from L.M.W. kininogen. No release of histamine was observed upon incubation with mast cells. |
| Quốc gia: | Portal de Revistas UCR |
| Tổ chức giáo dục: | Universidad de Costa Rica |
| Repositorio: | Portal de Revistas UCR |
| Ngôn ngữ: | Inglés |
| OAI Identifier: | oai:portal.ucr.ac.cr:article/24532 |
| Truy cập trực tuyến: | https://revistas.ucr.ac.cr/index.php/rbt/article/view/24532 |