Cloning and molecular characterization of BmHYA1, a novel hyaluronidase from the venom of Chinese red scorpion Buthus martensi Karsch.
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.
Feng
Luo
L
Venom and Toxin Research Programme, Department of Anatomy, Yong Loo Lin School of Medicine, National University of Singapore, 117597 Singapore, Singapore.
Gao
Rong
R
Meng
Jun
J
Gopalakrishnakone
Ponnampalam
P
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA; D018076:DNA, Complementary; D006821:Hyaluronoglucosaminidase / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D012604:Scorpion Venoms / Q000737:chemistry / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D012604:Scorpion Venoms; D004247:DNA; C532432:BmHYA1 protein, Buthus martensi; D006821:Hyaluronoglucosaminidase