Heavea latex lectin binding protein from the latex small rubber particles : purification and characterization

Heavea latex lectin binding protein from the latex small rubber particles : purification and characterization

Dhirayos Wititsuwannakul, Assoc. Prof., D. of Biochemistry, F. of Sci., Mahidol U., Bangkok
Kamonchanok Rukseree, D. of Biochemistry, F. of Sci., Mahidol U., Bangkok
Rapepun Wititsuwannakul, Assoc. Prof., D. of Biochemistry, F. of Sci., PSU.
Corresponding e-mail : wrapepun@ratree.psu.ac.th

Grant : Government Budget
Published : Research Report
Key words : Hevea brasiliensis, Euphobiaceae, rubber particle, lectin

A protein extracted from small rubber particles (SRP) obtained from the rubber layer of ultracentrifuged fresh latex in the presence of 0.2% Triton X-100 was able to bine Hevea latex lectin (HLL). The activity was measured from its ability to inhibit hemagglutination induced by HLL. The SRP-HLL binding protein (SRP-HLLBP) was purified from the extract by subjected to acetone precipitation, heat-treatment and gel filtration. Purified SRP-HLLBP possessed M_r of 120 and 24 kD upon native PAGE and SDS-PAGE, respectively. The pl value was determined to be 5.4 while pH optimum ranging from 5-8. It is heat stable upto 60^o. A decrease in hemagglutination inhibition (H.I.) was observed with chitinase-treated SRP-HLLBP. The specific H.I. titer observed with SRP-HLLBP was much lower than several other glycoproteins from non-latex origin.

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