Full TGIF Record # 25097
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Publication Type:
i
Report
Content Type:Abstract or Summary only
Author(s):Evenson, K. J.; Gengenbach, B. G.; Wyse, D. L.; Somers, D. A.; Gronwald, J. W.
Author Affiliation:Dep. Agron. and Plant Genetics, University of Minnesota: Research Assistant; Prof.; Assoc. Prof.; Prof.; Plant Physiol., Plant Sci. Res. Unit, U.S. Dep. Agric., Agric. Res. Serv.
Title:Purification and characterization of acetyl-coa carboxylase from diclofop-resistant and susceptible Italian ryegrass (Lolium multiflorum)
Meeting Info.:Held: December 10-12, 1991, Indianapolis, IN
Source:Proceedings of the North Central Weed Science Society. Vol. 46, 1991, p. 84.
# of Pages:1
Publishing Information:Omaha, NB: North Central Weed Control Conference
Keywords:TIC Keywords: Purity; Carboxylase; Substrates; Lolium multiflorum; Chromatography
Abstract/Contents:"Acetyl-CoA carboxylase (ACCase) was purified from green tissue of diclofop-resistant and susceptible biotypes of Lolium multiflorum. A 4-step purification including (NH4)2SO4 precipitation, sephacryl S400 chromatography and FPLC Mono-Q anion exchange chromatography resulted in a 122-fold purification and a specific activity of 3.0 units/mg protein for the susceptible biotype. The specific activity of the resistant biotype was slightly less (2.0 to 2.5 units/mg protein). Western blotting from SDS-PAGE gels and avidin binding demonstrated the enrichment of single biotinylated band of 200 KDa, corresponding to maximum ACCase activity. ACCase activity was also identified following native gradient PAGE by a malachite green assay. A green phosphate precipitate formed in this assay, but only in the presence of the substrate acetyl-CoA. Basic kinetics were determined for the three substrates utilized by ACCase, however no differences in Km values were observed between resistant and susceptible biotypes. Diclofop acted as a noncompetitive inhibitor of acetyl-CoA in the sensitive biotype with an I50 of 0.22 uM. The I50 for the resistant biotype was 2.5 uM. Free coenzyme A and malonyl-CoA both inhibited ACCase activity at millimolar concentrations."
Language:English
References:0
Note:This item is an abstract only!
ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete):
Evenson, K. J., B. G. Gengenbach, D. L. Wyse, D. A. Somers, and J. W. Gronwald. 1991. Purification and characterization of acetyl-coa carboxylase from diclofop-resistant and susceptible Italian ryegrass (Lolium multiflorum). Proc. North Cent. Weed Sci. Soc. 46:p. 84.
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