Purification, characterization and gene cloning of Da-36, a novel serine protease from Deinagkistrodon acutus venom.

@article{Zheng2013PurificationCA,
  title={Purification, characterization and gene cloning of Da-36, a novel serine protease from Deinagkistrodon acutus venom.},
  author={Ying Zheng and Feng-Ping Ye and Jie Wang and Guo-yang Liao and Yun Zhi Zhang and Quan-shui Fan and Wen-Hui Lee},
  journal={Toxicon : official journal of the International Society on Toxinology},
  year={2013},
  volume={67},
  pages={
          1-11
        }
}
A serine protease termed Da-36 was isolated from crude venom of Deinagkistrodon acutus. The enzyme was a single chain protein with an apparent molecular weight of 36,000 on SDS-PAGE with an isoelectric point of 6.59. Da-36 could clot human plasma by cleaving the Aα, Bβ and γ chains of fibrinogen and also exhibited arginine esterase activity. The proteolytic activity of Da-36 toward TAME was strongly inhibited by PMSF and moderately affected by benzamidine and aprotinin, indicating that it was a… CONTINUE READING

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