Journal
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-TOXICOLOGY & PHARMACOLOGY
Volume 148, Issue 3, Pages 250-257Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cbpc.2008.06.003
Keywords
hyaluronidase; scorpion venom; N-terminal sequence; CD44; purification
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A hyaluronidase, named BmHYA1, was purified from the venom of Chinese red scorpion (Buthus martensi), using successive chromatography. The homogeneity of BmHYA1 was confirmed by SDS-PAGE and MALDI-TOF mass spectrometry. The molecular mass of BmHYA1 was 48,696 Da determined by MALDI-TOF MS. The optimal temperature and pH of BmHYA1 were 50 degrees C and pH 4.5, respectively. It could be inhibited by DTT, Cu2+, Fe3+ or heparin, but not Mg2+, Ca2+, reduced glutathione, L-cysteine or EDTA. The sequence of thirty N-terminal amino acids of BmHYA1 was obtained by Edman degradation, as TSADF KVVWE VPSIM CSKKF KICVT DLLTS; but no similarity was found to other venom hyaluronidases. Further, BmHYA1 can hydrolyze hyaluronan into relatively smaller oligosaccharides and modulate the expression of CD44 variant in the breast cancer cell line MDA-MB-231. (C) 2008 Elsevier Inc. All rights reserved.
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