Isolation And Identification Of Toxin Peptides From Macropodia
Keywords
Spider Toxin Peptides From A. Giganticus Reversed-Phase High Performance Liquid Chromatography Mass Spectrometry Diversity
Abstract
Spiders are the most venomous animals, and the main component of their venom is toxin peptides rich in disulfide bonds. The main function of spider toxin peptides is to act on ion channels or receptors in the insect nervous system. The giant wart spider belongs to the order Araneae, the suborder Araneae, and the family Heterotheranidae. The crude venom of the tactile spider was separated by reversed-phase high-performance liquid chromatography, and then the molecular weight of each elution peak was determined by MALDI-TOF-TOF mass spectrometry. Experimental results show that a total of 108 types of toxin peptides were identified from the crude venom of A. tactata, with molecular weights ranging from 2 000 to 7 500 Da, with the main molecular weight range ranging from 2 000 to 4 500 Da (accounting for 63.9% ), and some are distributed in the range of 4 500 to 6 000 Da, while few are distributed in the range of 6 000 to 7 500 Da. Its molecular weight distribution characteristics are different from those of the reported prototheranids, reflecting the unique diversity of venom components of this spider.
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Original research done by 10.13610/j.cnki.1672-352x.20171017.020
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