Acid Phosphatase from Rat Liver
نویسندگان
چکیده
منابع مشابه
Acid Phosphatase from Rat Liver
Rat liver acid phosphatase (EC 3.1.3.2) was separated into two highly purified fractions, differing in isoelectric point and Km. One fraction was crystallized and proved homogeneous by ultracentrifugation and polyacrylamide gel electrophoresis. The molecular weights (lOO,OOO), substrate specificities, and pH optima of both enzymes were similar. Oxalate was a mixed type inhibitor to both enzymes...
متن کاملImmunocytochemical localization of acid phosphatase in rat liver.
Localization of acid phosphatase (ACPase) in rat liver was investigated by immunocytochemical techniques. Rat liver was fixed by perfusion and cut into thick tissue slices, which were embedded in Epon or Lowicryl K4M. For light microscopy (LM), semithin Epon sections were stained for the enzyme ACPase by an indirect immunoenzyme technique. For electron microscopy (EM), ultra-thin Lowicryl K4M s...
متن کاملStudies on kinetic properties of acid phosphatase from nuclei-free rat liver homogenate using different substrates.
Kinetic properties of rat liver acid phosphatase were evaluated using the conventional synthetic substrates sodium beta glycerophosphate (betaGP) and p-nitrophenyl phosphate (PNPP) and physiologically occurring phosphate esters of carbohydrates, vitamins and nucleotides. The extent of hydrolysis varied depending on the substrates; phosphate esters of vitamins and carbohydrates were in general p...
متن کاملSoluble and membrane-associated forms of acid phosphatase associated with the lysosomal fraction of rat liver.
As initially formulated (de Duve, 1959), the lysosome concept held that the hydrolytic enzymes associated with lysosomes are contained within the particles and that constraint from hydrolytic action is provided by the particle membrane, which acts as a barrier to enzyme-substrate interaction. Rupture of the lysosomal membrane, within this context, should result in the simultaneous release of al...
متن کاملThe effect of chick-liver ribonucleic acid on amino acid-incorporation systems from rat liver.
1. Rat-liver microsomes, ribonucleoprotein particles and a fraction mainly consisting of microsomal membranes were tested for their ability to incorporate amino acids into protein in the presence of ATP, GTP, phosphoenolpyruvate and pyruvate kinase. Addition of polyuridylic acid or of ribonucleic acid from rat-liver nuclei stimulated the incorporating activities. 2. These protein-synthesizing s...
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: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)94463-7