Your browser doesn't support javascript.
loading
Montrer: 20 | 50 | 100
Résultats 1 - 2 de 2
Filtre
1.
China Journal of Chinese Materia Medica ; (24): 4820-4829, 2019.
Article Dans Chinois | WPRIM | ID: wpr-1008169

Résumé

Agkistrodon acutus is a traditional Chinese herb medicine which has immunological regulation,anti-tumor,anti-inflammatory and analgesic effects,which is mainly used for the treatment of rheumatoid arthritis,ankylosing spondylitis,sjogren's syndrome and tumors. In order to excavate more important functional genes from A. acutus,the transcriptome of the venom gland was sequenced by the Illumina Hi Seq 4000,and 32 862 unigenes were assembled. Among them,26 589 unigenes were mapped to least one public database. 2 695 unigenes were annotated and assigned to 62 TF families,and 5 920 SSR loci were identified. The majority of mapped unigenes was from Protobothrops mucrosquamatus in the NR database,which revealed their closest homology. Three secretory phospholipase A_2 with different amino acid sequences showed similar spatial structures and all had well-conserved active sites. The 3 D structural models of C-type lectin showed conserved glycosylation binding sites( Asn45). This study will lay the foundation for the further study of the function of snake venom protein,and promoting the development and utilization of genome resources from A. acutus.


Sujets)
Animaux , Agkistrodon/génétique , Venins de crotalidé , Analyse de profil d'expression de gènes , Venins de serpent/génétique , Serpents , Transcriptome
2.
Indian J Exp Biol ; 2013 Dec; 51(12): 1063-1069
Article Dans Anglais | IMSEAR | ID: sea-150293

Résumé

The major hemorrhagin from C. purpureomaculatus (mangrove pit viper) venom was purified to homogeneity and termed Maculatoxin. Maculatoxin has a molecular weight of 38 kDa as determined by SDS-PAGE. It is an acidic protein (pI= 4.2) and exhibited proteolytic and hemorrhagic activities (MHD10 = 0.84 μg in mice) but was not lethal to mice at a dose of 1 μg/g. The hemorrhagic activity of Maculatoxin was completely inactivated by EDTA and partially inhibited by ATP and citrate. The N-terminal sequence of Maculatoxin (TPEQQRFPPTYIDLGIFVDHGMYAT) shares a significant degree of homology with the metalloprotease domain of other venom hemorrhagins. Indirect ELISA showed anti-Maculatoxin cross reacted with protein components of many snake venoms. In the double-sandwich ELISA, however, anti-Maculatoxin cross-reacted only with venoms of certain species of the Trimeresurus (Asia lance-head viper) complex, and the results support the recent proposed taxonomy changes concerning the Trimeresurus complex


Sujets)
Animaux , Chromatographie sur gel , Réactions croisées/immunologie , Endopeptidases/composition chimique , Endopeptidases/immunologie , Endopeptidases/isolement et purification , Souris , Masse moléculaire , Venins de serpent/génétique , Venins de serpent/immunologie , Spécificité d'espèce , Trimeresurus/immunologie , Trimeresurus/physiologie
SÉLECTION CITATIONS
Détails de la recherche