Vanadate Inhibition of Fungal PhyA and Bacterial AppA2 Histidine Acid Phosphatases

2011 ◽  
Vol 59 (5) ◽  
pp. 1739-1743 ◽  
Author(s):  
Abul H. Ullah ◽  
Kandan Sethumadhavan ◽  
Edward J. Mullaney
Keyword(s):  
Acid Phosphatases ◽  
Vanadate Inhibition

scholarly journals Vanadate inhibition of fungal and bacterial histidine acid phosphatases

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Abul H.J. Ullah ◽  
Kandan Sethumadhavan ◽  
Edward J Mullaney
Keyword(s):  
Acid Phosphatases ◽  
Vanadate Inhibition

Localization of acid phosphatases in root cap of rice plant

1991 ◽  
Vol 49 ◽  
pp. 224-225
Author(s):  
Y. R. Chen ◽  
Y. F. Huang ◽  
W. S. Chen
Keyword(s):  
Rice Plant ◽  
Developmental Stages ◽  
Uranyl Acetate ◽  
Root Cap ◽  
Plant Tissues ◽  
Acid Phosphatases ◽  
Root Tips ◽  
Buffer Solution ◽  
Cacodylate Buffer ◽  
Ethanol Series

Acid phosphatases are widely distributed in different tisssues of various plants. Studies on subcellular localization of acid phosphatases show they might be present in cell wall, plasma lemma, mitochondria, plastid, vacuole and nucleus. However, their localization in rice cell varies with developmental stages of cells and plant tissues. In present study, acid phosphatases occurring in root cap are examined.Sliced root tips of ten-day-old rice(Oryza sativa) seedlings were fixed in 0.1M cacodylate buffer containing 2.5% glutaraldehyde for 2h, washed overnight in same buffer solution, incubated in Gomori's solution at 37° C for 90min, post-fixed in OsO4, dehydrated in ethanol series and finally embeded in Spurr's resin. Sections were doubly stained with uranyl acetate and lead citrate, and observed under Hitachi H-600 at 75 KV.

The Demonstration of Human Prostatic Acid Phosphatase (Pap) With Phosphorylcholine

1976 ◽  
Vol 34 ◽  
pp. 88-89
Author(s):  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman
Keyword(s):  
Acid Phosphatase ◽  
Prostate Gland ◽  
Prostatic Acid Phosphatase ◽  
Human Prostate ◽  
Rat Tissues ◽  
Specific Substrate ◽  
Acid Phosphatases ◽  
Lysosomal Acid ◽  
Cacodylate Buffer

As previously reported (1, 2) phosphorylcholine (PC) is a specific substrate for prostatatic acid phosphatase (PAP) as opposed to other acid phosphatases, e.g., lysosomal acid phosphatase. The specificity of PC for PAP is due to the pentavalent nitrogen in PC, a feature that renders PC resistant to hydrolysis by all other acid phosphatases. Detailed comparative cytochemical results in rat tissues are in press. This report deals with ultracytochemical results applying the method to normal and pathological human prostate gland.Fresh human prostate was obtained from 7 patients having transurethral resections or radical prostatectomies. The tissue was fixed in 3% glutaraldehyde- 0.1 M cacodylate buffer (pH 7.4) for 15 min, sectioned at 50 μm on a Sorvall TC-2 tissue sectioner, refixed for a total of 2 hr, and rinsed overnight in 0.1 M cacodylate buffer (pH 7.4)-7.5% sucrose.

The role of acid phosphatases in plant phosphorus metabolism

1994 ◽  
Vol 90 (4) ◽  
pp. 791-800 ◽  
Author(s):  
Stephen M. G. Duff ◽  
Gautam Sarath ◽  
William C. Plaxton
Keyword(s):  
Phosphorus Metabolism ◽  
Acid Phosphatases

FeIIIFeIIIand FeIIFeIIIComplexes as Synthetic Analogues for the Oxidized and Reduced Forms of Purple Acid Phosphatases

1996 ◽  
Vol 35 (8) ◽  
pp. 2360-2368 ◽  
Author(s):  
Ademir Neves ◽  
Marcos A. de Brito ◽  
Ivo Vencato ◽  
Valderes Drago ◽  
Klaus Griesar ◽  
...  
Keyword(s):  
Acid Phosphatases ◽  
Synthetic Analogues ◽  
Purple Acid Phosphatases ◽  
Reduced Forms

Molecular weight differences in acid phosphatases of stem homogenates from L and S flax genotrophs

1983 ◽  
Vol 21 (3-4) ◽  
pp. 391-404 ◽  
Author(s):  
Mary Ann Fieldes ◽  
Hugh Tyson
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatases ◽  
Flax Genotrophs

The role of acid phosphatases in plant phosphorus metabolism

1994 ◽  
Vol 90 (4) ◽  
pp. 791-800 ◽  
Author(s):  
Stephen M. G. Duff ◽  
Gautam Sarath ◽  
William C. Plaxton
Keyword(s):  
Phosphorus Metabolism ◽  
Acid Phosphatases

scholarly journals Systematic synthesis of functional unsymmetric FeZn model complexes for plant purple acid phosphatases

2010 ◽  
Vol 13 (3) ◽  
pp. 334-337 ◽  
Author(s):  
Martin Jarenmark ◽  
Håkan Carlsson ◽  
Vladimir M. Trukhan ◽  
Matti Haukka ◽  
Sophie E. Canton ◽  
...  
Keyword(s):  
Acid Phosphatases ◽  
Model Complexes ◽  
Purple Acid Phosphatases ◽  
Systematic Synthesis

In vitro translation of human prostatic acid phosphatase mRNA and processing of the translation products by microsomal membranes and endoglycosidase H

1987 ◽  
Vol 65 (10) ◽  
pp. 921-924 ◽  
Author(s):  
Gilles Paradis ◽  
Jean Y. Dubé ◽  
Pierre Chapdelaine ◽  
Roland R. Tremblay
Keyword(s):  
Acid Phosphatase ◽  
Molecular Mass ◽  
Polyacrylamide Gel Electrophoresis ◽  
Prostatic Acid Phosphatase ◽  
In Vitro Translation ◽  
Acid Phosphatases ◽  
Major Band ◽  
Microsomal Membranes ◽  
Endoglycosidase H

Poly(A)+ RNA was isolated from human prostatic tissue and translated in vitro in a rabbit reticulocyte lysate translation assay. Acid phosphatase labeled with [35S]methionine was immunoprecipitated with an antibody against seminal plasma acid phosphatase. Two-dimensional polyacrylamide gel electrophoresis of the immunoprecipitate, followed by fluorography, revealed the presence of two spots (one major and one minor), both having a molecular mass of 43 kilodaltons (kDa) and an isoelectric point higher than mature acid phosphatase. Addition of canine pancreatic membranes to the translation assay resulted in the formation of four immunoprecipitable spots with molecular masses ranging from 43 to 49 kDa on one-dimensional gels. These spots probably represent acid phosphatases containing one to four core sugar groups, since after the addition of endoglycosidase H the molecular mass heterogeneity was abolished and we observed only one major band with a molecular mass (41 kDa) slightly lower than the ones of the primary translation product. These results suggest that human prostatic acid phosphatases are synthesized as two 43-kDa preproteins, which are further processed to 41-kDa proteins by removal of their signal peptide. Heterogeneity of the native protein arises mostly from glycosylation at four sites and not from differences in the amino acid sequence of the various forms.

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