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.

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.

Molecular and enzymatic characterization of acid phosphatase from venom of Scleroderma guani

2017 ◽  
Vol 20 (4) ◽  
pp. 1434-1441 ◽  
Author(s):  
Nai-Yong Liu ◽  
Xiao-Hong Fan ◽  
Zhi-Quan Zhang ◽  
Guo-Xing Wu ◽  
Jia-Ying Zhu
Keyword(s):  
Acid Phosphatase ◽  
Enzymatic Characterization

scholarly journals ACID PHOSPHATASE ACTIVITY IN INDIVIDUAL NEURONS DURING CHROMATOLYSIS: A QUANTITATIVE HISTOCHEMICAL STUDY

1970 ◽  
Vol 18 (11) ◽  
pp. 828-833 ◽  
Author(s):  
HILDE E. HIRSCH ◽  
THEODORE OBENCHAIN
Keyword(s):  
Spinal Cord ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Histochemical Study ◽  
Galactosidase Activity ◽  
Fluorogenic Substrates ◽  
Striking Increase ◽  
Staining Methods ◽  
Glucose 6 Phosphate Dehydrogenase

Two fluorogenic substrates, α-naphthyl phosphate and 4-methylumbelliferyl phosphate, were used to measure acid phosphatase activities in individual anterior horn neurons of the monkey spinal cord after section of the sciatic nerve. Although many studies utilizing staining methods have reported a striking increase in acid phosphatase activity during chromatolysis, no significant differences were observed here between the neurons of the operated and unoperated side, despite widespread chromatolysis. β-galactosidase activity was also unchanged, but the marked elevation of glucose 6-phosphate dehydrogenase during the reparative phase was confirmed.

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

Purification and enzymatic characterization of membrane-bound d-gluconate dehydrogenase from Arthrobacter globiformis

2015 ◽  
Vol 113 ◽  
pp. 14-22 ◽  
Author(s):  
Guifang Yang ◽  
Zhuan Wei ◽  
Wenjing Sun ◽  
Fengjie Cui ◽  
Daming Wang ◽  
...  
Keyword(s):  
Arthrobacter Globiformis ◽  
Enzymatic Characterization ◽  
Membrane Bound

Purification and characterization of a membrane-bound acid phosphatase of Leishmania mexicana

1991 ◽  
Vol 47 (1) ◽  
pp. 101-108 ◽  
Author(s):  
Beatrice Menz ◽  
Gerhard Winter ◽  
Thomas Ilg ◽  
Friedrich Lottspeich ◽  
Peter Overath
Keyword(s):  
Acid Phosphatase ◽  
Leishmania Mexicana ◽  
Purification And Characterization ◽  
Membrane Bound

Identification and partial characterization of an extracellular acid phosphatase activity of Leishmania donovani promastigotes

1982 ◽  
Vol 2 (1) ◽  
pp. 76-81
Author(s):  
M Gottlieb ◽  
D M Dwyer
Keyword(s):  
Acid Phosphatase ◽  
Leishmania Donovani ◽  
Surface Membrane ◽  
Extracellular Enzyme ◽  
Growth Cycle ◽  
Growth Media ◽  
Ph Optimum ◽  
Membrane Bound ◽  
Extracellular Acid Phosphatase

An extracellular acid phosphatase was detected in the growth media of Leishmania donovani promastigotes. The enzyme was released at all stages of the growth cycle and in amounts which accounted for 90% of the total amount of this enzyme in the culture. The exoenzyme exhibited a pH optimum of 4.5 to 5.0 and was active with a variety of organic phosphates. The enzymatic activity was excluded from Sephacryl S-300 and was retained by ultrafilters with nominal molecular weight cutoffs of up to 300,000. The results of comparative studies indicated that the extracellular enzyme was distinct from a surface membrane-bound acid phosphatase of L. donovani promastigotes which has been previously described.

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