scholarly journals Cadmium effects on the ratio of activities of lysosomal and total acid phosphatases (ACPLys/ACPTot) in Lymantria dispar larvae

2013 ◽  
Vol 65 (1) ◽  
pp. 345-352 ◽  
Author(s):  
Vlahovic Milena ◽  
Ilijin Larisa ◽  
Matic Dragana ◽  
Lazarevic Jelica ◽  
Nenadovic Vera ◽  
...  
Keyword(s):  
Lymantria Dispar ◽  
Acid Phosphatases ◽  
Total Acid

Total, tartrate-resistant, and tartrate-inhibited acid phosphatases in serum: biological variations and reference limits.

1988 ◽  
Vol 34 (4) ◽  
pp. 685-690 ◽  
Author(s):  
F Schiele ◽  
Y Artur ◽  
A Y Floc'h ◽  
G Siest
Keyword(s):  
Acid Phosphatase ◽  
Healthy Subjects ◽  
Acid Phosphatases ◽  
Alkaline Phosphatases ◽  
Total Acid ◽  
Factors Affecting ◽  
Reference Limits ◽  
Inhibited Acid ◽  
Main Factors ◽  
Apparently Healthy

Abstract We studied several factors affecting biological variation in serum acid phosphatases in a population of 1195 apparently healthy subjects four years old or older. We assayed total acid phosphatase activities in the presence of a transphosphorylating agent and using alpha-naphthyl phosphate as substrate. The main factors modifying total and tartrate-resistant acid phosphatases activities in serum are similar to those observed for total and bone alkaline phosphatases activities: age, sex, and hormonal state (puberty or menopause). The tartrate-inhibited acid phosphatase activity is, however, independent of biological variations. Finally, we propose reference limits for total, tartrate-resistant, and tartrate-inhibited acid phosphatases in serum.

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

Structure and chemical composition of exopolysaccharides of frost-damaged sugar beet

2020 ◽  
pp. 34-39
Author(s):  
Aneta Antczak-Chrobot ◽  
Maciej Wojtczak
Keyword(s):  
Spectral Analysis ◽  
Chemical Composition ◽  
Sugar Beet ◽  
Total Acid ◽  
Average Molecular Mass ◽  
Central European ◽  
Composition And Structure ◽  
Monomeric Composition ◽  
Branched Structure ◽  
Different Origin

In this research paper, development of a procedure of isolation of exopolysaccharides from frost-damaged beet and an analysis of structural and chemical composition of polymers isolated from sugar beet of different origin are presented. Total acid hydrolysis degradation integrated with HPAEC-ED analysis has been utilized to confirm the monomeric composition of the separated polysaccharides. The implementation of NMR spectral analysis and SEC chromatography of the structure of exopolysaccharides has been investigated. The results demonstrate that the chemical composition and structure of exopolysaccharides depend on their origin. Typical exopolysaccharides from Central European beet roots consist mainly of glucose monomers – and they have low branched structure – about 90% of α-1,6 linkage which is typical for dextran. The exopolysaccharides isolated from Swedish beet are characterized by 50–60% fructose monomers. They contain only about 65% α-1,6 linkages. Exopolysaccharides extracted from various origin beet differ in average molecular mass. The molecular distribution is not normal.

Sign in / Sign up

Export Citation Format

Share Document