The protein phosphatase 2As (PP2As) play a key role in manipulating protein phosphorylation. Although a number of proteins in the latex of laticifers are phosphorylated during latex regeneration in rubber tree, information about the PP2A family is limited. In the present study, 36 members of the
The tonoplast-bound ATPase of Hevea brasiliensis (caoutchouc tree) was solubilized with dichloromethan and purified 100-fold with two ammonium sulfate precipitation steps and a G-200 gel filtration step. The resulting ATPase activity eluted according to a molecular mass of approximately 200 kDa and
A structural characterization of natural rubber (NR) was carried out by a combination of selective enzymatic treatment and high-resolution characterization techniques. The nitrogenous groups in NR from Hevea brasiliensis have been regarded as an important factor governing cured rubber properties,
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