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Title: Characterizing guayule rubber transferase activity

Journal Article · · Plant Physiology, Supplement; (USA)
OSTI ID:6810319
;  [1]
  1. Arizona State Univ., Tempe (USA)

Rubber transferase (RuT) activity, measured as incorporation of {sup 14}C(isopentenyl pyrophosphate) (IPP) into rubber, was assayed in suspensions of rubber particles purified from bark tissue of Parthenium argentatum, Gray. Rubber particle suspensions (RSP) have high RuT activity which is not diminished by repeated washing of the particles, demonstrating the firm association of the enzyme system with the particles. RuT activity varied with line: 11591 yielded more rubber particles with a greater activity per particle, than did other lines tested. Variation in activity also varied with bark age and season. Activity rapidly declined at temperatures above 16{degree}C in line 593, but was more stable in RSP isolated form line 11591. IPP-incorporation depends upon the concentration of two substrates, IPP and the starter molecule farnesyl pyrophosphate (FPP). In lines 593 and 11591, 20 uM FPP saturated the enzyme present in 6 {times} 10{sup 10} particles {times} cm{sup {minus}3}, whereas about 1 mM IPP was required for saturation. Under saturating FPP, the apparent K{sub m} of RuT was about 250 uM.

OSTI ID:
6810319
Journal Information:
Plant Physiology, Supplement; (USA), Vol. 89:4; ISSN 0079-2241
Country of Publication:
United States
Language:
English