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Stabilisation of Particle Integrity and Particle Bound cis ‐Prenyl Transferase Activity in Stored, Purified Rubber Particles
Author(s) -
Cornish Katrina,
Bartlett Désirée L.
Publication year - 1997
Publication title -
phytochemical analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 72
eISSN - 1099-1565
pISSN - 0958-0344
DOI - 10.1002/(sici)1099-1565(199705)8:3<130::aid-pca346>3.0.co;2-0
Subject(s) - natural rubber , chemistry , hevea brasiliensis , transferase , prenylation , particle (ecology) , enzyme , biochemistry , organic chemistry , biology , ecology
Biochemical studies of rubber particle bound cis ‐prenyl transferase (rubber transferase, EC 2.5.1.20) activity have been complicated due to instability of the enzyme in purified rubber particles. Parthenium argentatum rubber transferase activity represents an extreme case of instability, which necessitated fresh preparation of enzymatically active particles from living plant tissue for every experiment. This problem was compounded because rubber transferase activity is environmentally induced in P. argentatum , and is only strongly active during the winter months thus restricting biochemical experimentation to this season. In this paper, we describe a method which permits long term storage of enzymatically active rubber particles of P. argentatum , and validate its use in two contrasting laticiferous rubber producing species, Hevea brasiliensis and Ficus elastica . © 1997 John Wiley & Sons, Ltd.