Purification and properties of alkaline phosphatase from boar seminal plasma

Purification and properties of alkaline phosphatase from rat chloroma.

Activity was determined by the rate of hydrolysis of 13-glycerophosphate on p-nitrophenyl phosphate (8). The determination with sodium 13-glycerophosphate was carried out as follows. The reaction mixture consisted of 0.05 M Tnis-HC1 (pH 10), 0.023 M sodium 13-glycerophosphate, 0.004 M MgCl2, and enzyme in a final volume of 2 ml. After incubation at 37° for 30 mm, 2 ml of 10% tnicbloroacetic ac...

Measurement of alkaline phosphatase in canine seminal plasma--an update.

In dogs, diagnosis of incomplete ejaculation and azoospermia can be made by measuring the activity of the enzyme alkaline phosphatase (AP) in seminal plasma. However, even though upper cut-off value of 5000 IU/l is given in the literature, results by different assays may vary considerably. Furthermore, no data exist concerning the stability of the enzyme during storage of frozen seminal plasma,...

Proteomics of boar seminal plasma

Purification of Alkaline Phosphatase

8. An increase in the rate of progression of the bands down the column decreases the sharpness of the bands. On 'Zeo-Karb 215' (40-60 mesh/in.) a rate ofprogression of 10-15 cm./hr. gave satisfactory results. 9. Equations have been derived permitting the calculation ofthe proportion ofthe column occupied by a component, the width ofthe boundaries and the expected yield of pure components in sep...

Purification and Properties of Alkaline Phosphatase with Protein Phosphatase Activity from Saccharomyces cerevisiae

An alkaline phosphatase (A LPase) from Saccharomyces cerevisiae strain 257 was purified 345-fold with specific activity of 54 533 nmol x min“ 1 x mg protein-1 . It was shown to be a dimeric protein (apparent mol. wt. approx. 130 kDa) with optimum activity at pH 8.6 8.8 and good stability at 50 °C. The A LPase was a non-specific enzyme hydrolyzing a wide vari­ ety of monophosphate esters. The en...