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Digitale Medien

Purification of rat liver soluble catechol-O-methyltransferase by high performance liquid chromatography (1989)

Korkolainen, Tapio ; Nissinen, Erkki

New York, NY : Wiley-Blackwell

Biomedical Chromatography 3 (1989), S. 127-130

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Details

ISSN: 0269-3879

Schlagwort(e): Chemistry ; Analytical Chemistry and Spectroscopy

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Medizin

Notizen: The soluble form of catechol-O-methyltransferase (EC 2.1.1.6.) from rat liver was purified to homogeneity by high-performance anion-exchange chromatography and high-performance gel-filtration chromatography. The specific activity of the final pool was 270 U/mg protein. The purification was 1180-fold and recovery of the enzyme activity was 15%. During this rapid and gentle purification there were no problems with loss of activity, and the estimated half life of the final purified enzyme pool was 5.5 days at +4°C. The only additive used was phenylmethylsulfonylfluoride in the homogenizing buffer.

Zusätzliches Material: 3 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/bmc.1130030308

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