We have recently characterized a natural rubber in the latex of Euphorbia characias. Following that study,
we here investigated the rubber particles and rubber transferase in that Mediterranean shrub. Rubber
particles, observed by scanning electron microscopy, are spherical in shape with diameter ranging from
0.02 to 1.2 mm. Washed rubber particles exhibit rubber transferase activity with a rate of radiolabeled
[14C]IPP incorporation of 4.5 pmol min1 mg1.
Denaturing electrophoresis profile of washed rubber particles reveals a single protein band of 37 kDa
that is recognized in western blot analysis by antibodies raised against the synthetic peptide whose
sequence, DVVIRTSGETRLSNF, is included in one of the five regions conserved among cis-prenyl chain
elongation enzymes.
The cDNA nucleotide sequence of E. characias rubber transferase (GenBank JX564541) and the deduced
amino acid sequence appear to be highly homologous to the sequence of several plant cisprenyltransferases
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