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ARS Home » Midwest Area » West Lafayette, Indiana » Crop Production and Pest Control Research » Research » Publications at this Location » Publication #82262
Title: PURIFICATION OF SOYBEAN ACETYL COA CARBOXYLASE

Author
item REVERDATTO, SERGEY - PURDUE UNIVERSITY
item BEILINSON, VADIM - PURDUE UNIVERSITY
item NIELSEN, NIELS

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 6/30/1997
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: The chloroplast acetyl-CoA carboxylase (MS-ACCase, EC 6.4.1.2) from soybean is a multi-subunit complex that catalyzes the ATP-dependent formation of malonyl CoA. Clones encoding each type of soybean MS-ACCase have been isolated. Anti-bodies produced against E. coli expressed portions of each subunit were applied towards an investigation of the properties of soybean MS-ACCase. We show that multiple gene copies for alpha-CT and BCCP in soybean genome correlate with multiple proteins in soybean seed extracts. The initial dissociation of soybean MS-ACCase in high salt results in formation of BC/BCCP and alpha/beta-CT complexes with the loss of ACCase activity. Activity can be restored when appropriate purified fractions are mixed. The stability of subunit pairs permitted their purification by an affinity and antibody matrix chromatography targeted against individual members of the complex. Results of our studies about soybean MS-ACCase and dthe expression of MS-ACCase subunits in E. coli will be described.