Purification and Properties of Reactivated Alkaline Phosphatase from Goat Milk
نویسندگان
چکیده
منابع مشابه
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...
متن کاملAlkaline Phosphatase of Milk
inor i8obutanol. Removal of the lipid is accompanied by simultaneous release of the enzyme into true solution. No other organic solvent tested was effective in releasing the bound phosphatase, indicating a unique action of butanol. I wish to thank Dr M. Dixon, F.R.S., for his encouraging interest and advice during this work. This work was carried out while holding a Travelling Scholarship award...
متن کاملPurification 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...
متن کاملPurification 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...
متن کاملPurification and properties of bovine synovial fluid alkaline phosphatase.
Alkaline phosphatase from bovine synovial fluid was purified 2300-fold. A molecular weight of 72,300 was determined from sucrose density gradient studies. The following monoesters were hydrolyzed by the enzyme: P-glycerophosphate, galactosamine 6-phosphate, glucosamice 6-phosphate, glucose 6-phosphate, o-phospho-L-serine, o-carboxyphenyl phosphate, phenyl phosphate, and p-nitrophenyl phosphate....
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nihon Chikusan Gakkaiho
سال: 1981
ISSN: 1346-907X,1880-8255
DOI: 10.2508/chikusan.52.659