Purification and physicochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity

Biochemistry ◽  
1988 ◽  
Vol 27 (12) ◽  
pp. 4265-4273 ◽  
Author(s):  
Abdul Waheed ◽  
Piotr M. Laidler ◽  
Yu Yuan P. Wo ◽  
Robert L. Van Etten
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Protein Phosphatase ◽  
Physicochemical Characterization

scholarly journals Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A.

1994 ◽  
Vol 269 (22) ◽  
pp. 15668-15675 ◽  
Author(s):  
X. Cayla ◽  
C. Van Hoof ◽  
M. Bosch ◽  
E. Waelkens ◽  
J. Vandekerckhove ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Phosphatase Activity ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Phosphatase 2A

Characterization of major protein phosphatases from selected species of Kluyveromyces. Comparison with protein phosphatases from Yarrowia lipolytica

2001 ◽  
Vol 47 (9) ◽  
pp. 861-870 ◽  
Author(s):  
Pascale Jolivet ◽  
Edith Bergeron ◽  
Haguith Benyair ◽  
Jean-Claude Meunier
Keyword(s):  
Acid Phosphatase ◽  
Yarrowia Lipolytica ◽  
Protein Phosphatase ◽  
Protein Phosphatases ◽  
Major Protein ◽  
Ethanol Treatment ◽  
Early Stationary Phase ◽  
Yeast Strains ◽  
Deficient Medium

Casein phosphatase activities have been identified in five yeast strains grown on Pi-deficient medium. Maximal endocellular activities appeared in the exponential phase. Exocellular phosphatases were significantly produced from Yarrowia lipolytica W-29 and Kluyveromyces marxianus, in the early stationary phase. Major phosphatases from K. marxianus were one heavy acid phosphatase composed of 64–67 kDa subunits, which could be secreted in the medium, and one type 2A protein phosphatase with an apparent molecular mass of 147 kDa and a 52 kDa catalytic subunit dissociated by 80% ethanol treatment. The characteristics of phosphatases purified from K. marxianus were compared with those previously purified from Y. lipolytica.Key words: yeast, type 2A protein phosphatase, acid phosphatase, [32P]casein, Pi deficiency.

Characterization of phosphotyrosyl-protein phosphatase activity associated with calcineurin

1984 ◽  
Vol 121 (1) ◽  
pp. 141-148 ◽  
Author(s):  
Jonathan Chernoff ◽  
Mary Ann Sells ◽  
Heng-Chun Li
Keyword(s):  
Phosphatase Activity ◽  
Protein Phosphatase

Acid phosphatase in Gaucher's disease.

1980 ◽  
Vol 26 (3) ◽  
pp. 371-382
Author(s):  
D B Robinson ◽  
R H Glew
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Purification And Characterization ◽  
Gaucher's Disease ◽  
Gaucher’S Disease ◽  
Intracellular Location ◽  
Increased Activity ◽  
Serum Acid Phosphatase

Abstract Increased acid phosphatase activity in the serum and tissues of patients with Gaucher's disease has now been recognized for two decades, but as yet no relation has been established between the enzyme and the etiology and progress of the disease. Here, we review results obtained by various investigators, ranging from a consideration of the methods used for the evaluation of serum acid phosphatase in Gaucher's disease to the most recent findings regarding the purification and characterization of two acid phosphatase isoenzymes from the spleen from patients with Gaucher's disease. We also discuss the intracellular location of tissue acid phosphatase in patients with Gaucher's disease and its contribution to the increased activity in serum.

scholarly journals Purification and Characterization of a Potato Tuber Acid Phosphatase Having Significant Phosphotyrosine Phosphatase Activity

1994 ◽  
Vol 106 (1) ◽  
pp. 223-232 ◽  
Author(s):  
K. S. Gellatly ◽  
GBG. Moorhead ◽  
SMG. Duff ◽  
D. D. Lefebvre ◽  
W. C. Plaxton
Keyword(s):  
Acid Phosphatase ◽  
Potato Tuber ◽  
Phosphatase Activity ◽  
Purification And Characterization ◽  
Phosphotyrosine Phosphatase

Structural and enzymatic characterization of plant zymogen bodies

1971 ◽  
Vol 49 (11) ◽  
pp. 2053-2057 ◽  
Author(s):  
Esther Cohen ◽  
Y. Shain ◽  
Y. Ben-Shaul ◽  
A. M. Mayer
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Galactosidase Activity ◽  
Enzymatic Characterization ◽  
Subcellular Organelles ◽  
Inactive Form ◽  
Optimum Ph ◽  
Membrane Bound ◽  
Pea Seeds

The zymogen body fraction of pea seeds was further investigated as to the content and localization of additional enzymes. This fraction was previously shown to contain an inactive form of amylopectin-1,6-glucosidase. An acid phosphatase was found with an optimum pH of 5.4. ATP or GTP were the preferred natural substrates, although there was no effect of Mg2+, K+, or Na+ ions on this acid nucleotide phosphatase activity. Cytochemical methods show that the ATPase is membrane-bound and that these bodies have only a single limiting membrane. No RNAse activity could be found; however, there was considerable β-galactosidase activity. It is concluded that these zymogen bodies are a distinct class of subcellular organelles in plants.

Studies on host specificity in Paragonimus westermani: II. Histochemical and cytochemical characterization of metacercariae and worms from rats and dogs

1989 ◽  
Vol 63 (4) ◽  
pp. 315-327 ◽  
Author(s):  
Takahiro Fujino ◽  
Koichi Fukuda ◽  
Fusanori Hamajima ◽  
Yoichi Ishii
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Atpase Activity ◽  
Phosphatase Activity ◽  
Metabolic Activity ◽  
Acid And Alkaline Phosphatase ◽  
Excretory Bladder ◽  
Histochemical Tests ◽  
Parenchymal Cells

ABSTRACTHistochemical tests were done on newly excysted metacercariae and worms recovered from an abnormal host (rat) and the definitive host (dog) for some oxidoreductases, phosphatases and glycosidases. The results demonstrate that rat worms have enzymatic distribution and intensities more similar to those of metacercariae than to adult worms from dogs. Ultracytochemical examination of acid and alkaline phosphatase and Mg-ATPase activity was also carried out. Acid phosphatase activity occurred exceptionally in the excretory bladder and caeca of dog worms. No activity was observed in rat worms except for lysosomal granules in the tegument. Alkaline phosphatase activity was exhibited in the excretory bladder in both dog and rat worms. Mg-ATPase activity occurred in the tegument and parenchymal cells in dog worms and in the excretory bladder in rat worms. In metacercariae, little or no reaction for these enzymes was present except for Mg-ATPase activity on the excretory ducts. These observations, together with the histochemical results, indicate that metabolic activity in rat worms is higher than in metacercariae although it is strongly reduced compared with dog worms.

Sign in / Sign up

Export Citation Format

Share Document