Abstract
Interactions between human seminal acid phosphatase (AcP) and five kinds of lectins were studied. Seminal plasma was mixed with the lectins at various ratios. The mixtures were centrifuged and the supernatants were assayed for AcP activity. The activity was effectively reduced only with Canavalia gladiata DC (CG) lectin. CG lectin purified by Sephadex G-200 gel filtration was added to two fractions of AcP separated by Sephadex G-200 gel filtration. There was no difference in the rate of reduction of the two fractions. To isolate seminal AcP by affinity chromatography, CG lectin was coupled to agarose gel. AcP bound with the agarose gel could be eluted with alpha-methyl-D-mannoside. Specific activity of the purified AcP was elevated to as much as 54-fold.
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