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|Title:||Cloning and molecular characterization of BmHYA1, a novel hyaluronidase from the venom of Chinese red scorpion Buthus martensi Karsch||Authors:||Feng, L.
|Keywords:||3' RACE PCR
Full protein sequence
Scorpion venom hyaluronidase
|Issue Date:||2010||Citation:||Feng, L., Gao, R., Gopalakrishnakone, P., Meng, J. (2010). Cloning and molecular characterization of BmHYA1, a novel hyaluronidase from the venom of Chinese red scorpion Buthus martensi Karsch. Toxicon 56 (3) : 474-479. ScholarBank@NUS Repository. https://doi.org/10.1016/j.toxicon.2010.04.009||Abstract:||In this communication, the full protein sequence of a novel venom hyaluronidase BmHYA1 was reported. It is the first full hyaluronidase amino acid sequence from scorpion venom. It was deduced from nucleotide sequence by 3' Rapid Amplification of cDNA Ends (RACE) PCR cloning, followed by alignment with the N-terminal amino acid sequence, which was obtained by Edman degradation. BmHYA1 has 385 amino acid residues containing five potential N-glycosylation sites. The phylogenetic analysis indicates early divergence and independent evolution of BmHYA1 from other hyaluronidases. © 2010 Elsevier Ltd.||Source Title:||Toxicon||URI:||http://scholarbank.nus.edu.sg/handle/10635/24318||ISSN:||00410101||DOI:||10.1016/j.toxicon.2010.04.009|
|Appears in Collections:||Staff Publications|
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