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Purification of Bovine Plasma Arylesterase^1,2,

Department of Animal Sciences, Washington State University, Pullman

ABSTRACT

Bovine plasma arylesterase was purified by: 1) precipitation between 50 and 75% saturation with (NH₄)₂SO₄ at 0 C, 2) chromatography of a solution of the precipitate on Sephadex G-200, 3) rechromatography of the pooled enzyme fractions on DEAE-cellulose at pH 7.8, and 4) removal of a precipitate formed when the pooled fractions from (3) above were concentrated and stored at 3–5 C for a week. The purified preparation had a specific activity of 137 µmoles phenyl acetate hydrolyzed per minute per milligram protein which represented more than 180-fold purification. Electrophoretic studies of this preparation on cellulose polyacetate strips showed the presence of only one homogeneous component.

¹ College of Agriculture Scientific Paper no. 2925. Work conducted under project 1597. This investigation was supported in part by funds provided for biological and medical research by the State of Washington Initiative Measure no. 171.

² Data in this paper are from a thesis submitted by the senior author in partial fulfillment of the requirements for the degree of Doctor of Philosophy.