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. 1980 Feb;141(2):544–549. doi: 10.1128/jb.141.2.544-549.1980

Stabilization and purification of ornithine transcarbamylase from Neisseria gonorrhoeae.

C N Powers, D L Pierson
PMCID: PMC293657  PMID: 6767684

Abstract

Ornithine transcarbamylase was stabilized in cell-free extracts by the presence of either carbamyl phosphate or glycerol. The enzyme was rapidly purified by a procedure consisting of ion-exchange chromatography and electrofocusing. The native molecular weight of the enzyme was determined by gel filtration to be 110,000. A subunit molecular weight of 36,000 was determined by polyacrylamide electrophoresis under dissociating conditions. These findings indicated a trimeric quaternary structure for the enzyme. The isoelectric point of the purified enzyme was 4.75, and no evidence of multiple forms of active enzyme was found in either crude or purified preparations. An inactive form of the enzyme appeared upon storage in the absence of stabilization buffer.

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Selected References

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