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Agkihpin, a Distinct SVTLE from the Venom of Gloydius halys Pallas : Purification, Characterization and Structure–Activity Determination
Author(s) -
Tang Yulu,
Huang Miao,
Hu Qiping,
Wu Huayu,
Yao Jiali,
Sun Kejian,
Li Xiaolong
Publication year - 2018
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.201800122
Subject(s) - viperidae , chemistry , venom , snake venom , biochemistry , amino acid , molecular mass , enzyme
Blood clots produced by snake‐venom thrombin‐like enzymes ( SVTLE s) are cleared rapidly, which makes SVTLE s attractive as potential candidates for antithrombotic therapy. We isolated a SVTLE , agkihpin, from the venom of Gloydius halys Pallas . Agkihpin was confirmed to a single‐chain TLE with molecular mass of 25.5 kD , pI of 7.43, optimal pH of 8.0 (hydrolyzing TAME ), linked carbohydrate absent, and weak fibrinogen clotting activity. It was also found that (i) G . halys might be the latest species in SVTLE s phylogenetic tree; (ii) different level of conservation was shown among the SVTLE s from the Viperidae snakes. Some of those site may account for different activities exhibited by those SVTLE s, especially position 181, at which a fibrinogenolytic activity increase was found when a basic and larger amino acid substituted by a neutral and smaller one; (iii) an extra α ‐helix constructed with a ‘Pro + acidic amino acid + aromatic amino acid’ pattern was found in the SVTLE s from Gloydius and Agkistrodon snakes, although it does not necessarily imply an effect on the fibrinogenolytic activity of the SVTLE s. This study provided some new insight into the activity of SVTLE.