Acid Phosphatase During Development of the Black Carpet Beetle Attagenus megatoma (Fab.)

1971 ◽  
Vol 49 (3) ◽  
pp. 311-315 ◽  
Author(s):  
J. Nath ◽  
L. Butler
Keyword(s):  
Acid Phosphatase ◽  
Specific Activity ◽  
Pupal Stage ◽  
Age Dependent ◽  
Black Carpet Beetle

The specific activity for free and bound fractions of acid phosphatase revealed age-dependent alterations during the development of the black carpet beetle, Attagenus megatoma (Fab.). Both fractions exhibited highest activity at the pupal stage. The specific activity appears to be related to the biology of the organism.

STUDIES ON THYROIDAL COLLOID PINOCYTOSIS USING A DOUBLE ISOTOPE TECHNIQUE

1972 ◽  
Vol 70 (1) ◽  
pp. 48-55 ◽  
Author(s):  
Mario A. Pisarev ◽  
Noe Altschuler ◽  
Leslie J. DeGroot
Keyword(s):  
Acid Phosphatase ◽  
Thyroid Hormone ◽  
Trichloroacetic Acid ◽  
Specific Activity ◽  
Acid Precipitation ◽  
Solvent System ◽  
Blood Stream ◽  
Radioactive Materials ◽  
Isotope Technique ◽  
Double Isotope

ABSTRACT The process of secretion of the thyroid hormone involves several steps: pinocytosis of thyroglobulin, fusion of the colloid droplets with the lysosomes, digestion of thyroglobulin by a cathepsin, dehalogenation of tyrosines and release of thyronines into the blood stream. The present paper describes a double isotope technique for studying the first two steps. Thyrotrophin (TSH) administration to rats increased the radioactivity present in all fractions, specially in the 15 000 × g pellet. When the subcellular distribution of acid phosphatase was determined, the highest specific activity was found in this fraction, thus indicating the presence of lysosomes. The content of radioactive materials in the 15 000 × g pellet was analyzed by trichloroacetic acid precipitation and by ascending paper chromatography using n-butanol:ethanol:ammonium hydroxide (5:1:2;v/v) as solvent system. The results obtained showed that 90% of the radioactivity was protein bound and strongly suggest that this material is thyroglobulin.

scholarly journals Assessment of Acid Phosphatase Production by In vitro Cultures of Atropa acuminata

2016 ◽  
Vol 26 (1) ◽  
pp. 15-23
Author(s):  
Saima Khan ◽  
Meenu Katoch ◽  
Sharada Mallubhotla ◽  
Suphla Gupta ◽  
Manju Sambyal ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Growth Period ◽  
Callus Cultures ◽  
Shoot Cultures ◽  
Crude Enzyme Extract ◽  
Atropa Acuminata

The potential of various culture lines of Atropa acuminata were investigated for resourcing acid phosphatase (ACP) (3.1.3.2). Crude enzyme extract comprised of a mixture of four isoforms, distinguishable by polyacrylamide gel electrophoresis (PAGE) with molecular weight ranging from 39 to 215 kDa. In vitro regenerated proliferative shoots, callus and roots showed higher specific activity (2.49, 3.41, 2.91 U/mg protein, respectively) as compared to in vivo grown plants (0.71 U/mg protein). ACP activity in root cultures increased progressively up to 4.6 U/mg during the entire growth period (2 ? 24 weeks), whereas in case of shoot cultures, the specific activity escalated to 2.49 U/mg at 8 weeks, which then declined subsequently (1.95 U/mg). Similarly, callus cultures initially showed a higher phosphohydrolytic activity (3.41 U/mg protein) until 8 weeks by which period, it decreased with the passage of growth period. The present studies reveal an alternate system for resourcing of ACP from Atropa acuminata.Plant Tissue Cult. & Biotech. 26(1): 15-23, 2016 (June)

scholarly journals [Phosphotyrosine]protein phosphatase in rat brain. A major [phosphotyrosine]protein phosphatase is a 23 kDa protein distinct from acid phosphatase

1986 ◽  
Vol 239 (1) ◽  
pp. 155-162 ◽  
Author(s):  
M Okada ◽  
K Owada ◽  
H Nakagawa
Keyword(s):  
Acid Phosphatase ◽  
Molecular Mass ◽  
Rat Brain ◽  
Column Chromatography ◽  
Protein Phosphatase ◽  
Specific Activity ◽  
Deae Cellulose ◽  
Sodium Vanadate ◽  
Nitrophenyl Phosphate ◽  
Phosphotyrosine Protein Phosphatase

A [phosphotyrosine]protein phosphatase (PTPPase) was purified almost to homogeneity from rat brain, with [32P]p130gag-fps, an oncogene product of Fujinami sarcoma virus, as substrate. The characteristics of the purified preparation of PTPPase were as follows: the enzyme was a monomer with a molecular mass of 23 kDa; its optimum pH was 5.0-5.5; its activity was not dependent on bivalent cations; its activity was strongly inhibited by sodium vanadate, but was not inhibited by ZnCl2, L(+)-tartrate or NaF; it catalysed the dephosphorylation of [32P]p130gag-fps, [[32P]Tyr]casein, p-nitrophenyl phosphate and L-phosphotyrosine, but did not hydrolyse [[32P]Ser]tubulin, L-phosphoserine, DL-phosphothreonine, 5′-AMP, 2′-AMP or beta-glycerophosphate significantly. During the purification, most of the PTPPase activity was recovered in distinct fractions from those of conventional low-molecular-mass acid phosphatase (APase), which was reported to be a major PTPPase [Chernoff & Li (1985) Arch. Biochem. Biophys. 240, 135-145], from DE-52 DEAE-cellulose column chromatography, and those two enzymes could be completely separated by Sephadex G-75 column chromatography. APase also showed PTPPase activity with [32P]p130gag-fps, but the specific activity was lower than that of PTPPase with molecular mass of 23 kDa, and it was not sensitive to sodium vanadate. These findings suggested that PTPPase (23 kDa) was the major and specific PTPPase in the cell.

scholarly journals Analytical subcellular fractionation of alveolar macrophages from normal and BCG-vaccinated rabbits with particular reference to heterogeneity of hydrolase-containing granules

1979 ◽  
Vol 178 (3) ◽  
pp. 761-767 ◽  
Author(s):  
D B Lowrie ◽  
P W Andrew ◽  
T J Peters
Keyword(s):  
Acid Phosphatase ◽  
Specific Activity ◽  
Sucrose Density Gradient ◽  
Subcellular Fractionation ◽  
Equilibrium Density ◽  
Type B ◽  
Type C ◽  
Pulmonary Granulomas ◽  
B Granules ◽  
Isopycnic Centrifugation

Macrophages were obtained by pulmonary lavage from normal rabbits or rabbits that had developed pulmonary granulomas after receiving intravenous BCG vaccine 2-3 weeks earlier. The cells were disrupted in iso-osmotic sucrose and a low-speed supernatant was fractionated by isopycnic centrifugation on a linear sucrose density gradient. Three populations of hydrolase-containing granules (putative lysosomes) were found in both normal and BCG-induced macrophages. They were distinguished by their different distributions in the gradient and different sensitivities to disruption by digitonin and were termed:type A, containing lysozyme; type B, containing N-acetyl-beta-glucosaminidase, beta-glactosidase, beta-glucuronidase and possibly some lysozyme; type C, containing cathepsin D. Acid phosphatase appeared to be about equally distributed between type B and C granules. Type A and B granules from BCG-induced macrophages showed markedly greater equilibrium density than did those from normal macrophages. Beta-glucuronidase and acid phosphatase had greater specific activity in the induced cells.

EFFECTS OF 5α-ANDROSTANE-3β,17β-DIOL AND 5β-DIHYDROTESTOSTERONE ON ACID PHOSPHATASE ACTIVITY IN THE PROSTATE GLAND OF THE CASTRATED ADULT RAT

1978 ◽  
Vol 79 (1) ◽  
pp. 9-16 ◽  
Author(s):  
M. P. TENNISWOOD ◽  
PAMELA P. ABRAHAMS ◽  
C. E. BIRD ◽  
A. F. CLARK
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Prostate Gland ◽  
Intraperitoneal Administration ◽  
Adult Rat ◽  
Secretory Acid Phosphatase

Polyacrylamide gel electrophoresis of filtrates from adult rat prostatic tissue showed two bands of acid phosphatase activity. These corresponded to the lysosomal and secretory acid phosphatases. After castration the secretory acid phosphatase disappeared. The specific activity of the enzyme increased from the time of castration to a maximum on day 7 before declining steadily, while the percentage inhibition by tartrate of acid phosphatase increased from control levels to a maximum on day 7 and then decreased to a new steady state by day 15. When 5α-androstane-3β,17β-diol was administered i.p. at a dose of 2 mg/day, starting immediately after castration, the secretory acid phosphatase was retained but the percentage inhibition and the specific activity were both raised above control levels. When this steroid was administered daily starting 7 days after castration the secretory acid phosphatase band on the gels returned more rapidly than with the classical androgens, but the percentage inhibition and specific activity were once again raised. Intraperitoneal administration of 5β-dihydrotestosterone, at a dose of 2 mg/day, did not maintain the secretory acid phosphatase activity which disappeared by day 5. However, the specific activity of acid phosphatase and the percentage inhibition by tartrate were both raised throughout the experiment. If this steroid was given 7 days after castration, the percentage inhibition by tartrate did not respond and fell to the level seen in castrated rats. The specific activity, however, remained significantly above the level found in castrated control rats.

scholarly journals BETA GLUCURONIDASE-RICH CYTOPLASMIC PARTICLES IN ANDROGEN-STIMULATED MOUSE KIDNEY

1963 ◽  
Vol 16 (2) ◽  
pp. 253-258 ◽  
Author(s):  
Andrew G. Plaut ◽  
William H. Fishman
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Specific Activity ◽  
Mouse Kidney ◽  
The Other ◽  
Mouse Testis ◽  
Glucuronidase Activity ◽  
Other Hand ◽  
Fraction I ◽  
Gonadotropic Hormones

Androgens produced by stimulating mouse testis with gonadotropic hormones cause a rise in renal ß-glucuronidase but not an increase in acid or alkaline phosphatase. All subcellular components increase in ß-glucuronidase activity, with a relatively greater increment in particulate enzyme as compared with that free in the cytoplasm (non-sedimentable). A small percentage of recovered ß-glucuronidase, acid phosphatase, and alkaline phosphatase is found in material which rises to the surface during centrifugation in sucrose media (fraction I). The specific activity of ß-glucuronidase and acid phosphatase in this fraction is normally quite high with respect to the homogenate, while that of alkaline phosphatase is not. On the other hand, the fraction I material from androgen-stimulated mice exhibits a further increase in specific activity with respect to ß-glucuronidase and not acid phosphatase. It thus appears that there is an independence in the behavior of individual enzymes in response to physiologic stimuli in spite of obvious morphologic proximity.

scholarly journals Clinical Significance of Immunoassays for Type-5 Tartrate-resistant Acid Phosphatase

1999 ◽  
Vol 45 (12) ◽  
pp. 2150-2157 ◽  
Author(s):  
Yuri R Nakasato ◽  
Anthony J Janckila ◽  
Jussi M Halleen ◽  
H Kalervo Vaananen ◽  
Stephanie P Walton ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Rheumatic Disease ◽  
Healthy Subjects ◽  
Specific Activity ◽  
Biological Significance ◽  
Tartrate Resistant Acid Phosphatase ◽  
Endstage Renal Disease ◽  
Trap Activity ◽  
Specificity And Sensitivity ◽  
The Mean

Abstract Background: Tartrate-resistant acid phosphatase (TRAP; EC 3.1.3.2) is a product of osteoclasts and a biochemical marker of bone resorption rate. However, erythrocytes and platelets contribute to total TRAP activity in serum, reducing the specificity of direct biochemical assays in serum. Osteoclast TRAP is also known as type-5 TRAP and is antigenically unique. Immunoassays are sought to improve the specificity and sensitivity of TRAP as a bone marker. Methods: We developed two colorimetric microplate assays for type-5 TRAP: an enzyme capture immunoassay to measure antibody-bound enzymatic activity, and a two-site immunoassay to measure bound enzyme protein. Both use the same monoclonal antibody (14G6) to capture type-5 TRAP, which permits determination of specific activity of serum TRAP in health and disease. Results: Both TRAP assays were linear from one-tenth to fivefold the mean value in 18 healthy subjects. In these subjects, the mean (SD) TRAP activity was 3.2 (0.54) U/L for the enzyme capture assay and 37 (13) μg/L for the two-site assay. Mean TRAP activity was not significantly increased in 64 patients with endstage renal disease requiring hemodialysis (HD) or 99 unselected patients with rheumatic diseases. By contrast, TRAP protein was increased in both the HD and rheumatic disease groups. The specific activity of TRAP in the 17 of 64 HD sera that had increased TRAP activity (0.088 U/μg) was similar to that in healthy subjects (0.091 U/μg). By contrast, the specific activity of TRAP in the 31 of 99 rheumatic sera with increased TRAP protein (0.035 U/μg) was significantly decreased. Conclusions: Wide sample distributions for TRAP activity in HD patients and TRAP protein in rheumatic disease patients suggest the presence of subpopulations of HD patients with increased TRAP activity and of rheumatic patients with increased TRAP protein. Each assay for TRAP activity and protein may have its own biological significance and clinical applications in specific groups of patients.

Maturation enhances fluid shear-induced activation of eNOS in perfused ovine carotid arteries

2005 ◽  
Vol 289 (5) ◽  
pp. H2220-H2227 ◽  
Author(s):  
Charles Ray White ◽  
Mohammad Wael Hamade ◽  
Koushan Siami ◽  
Melody M. Chang ◽  
Anandit Mangalwadi ◽  
...  
Keyword(s):  
Shear Stress ◽  
Surface Area ◽  
Carotid Arteries ◽  
Fluid Shear Stress ◽  
Specific Activity ◽  
Luminal Surface ◽  
Fluid Shear ◽  
No Release ◽  
Age Dependent ◽  
Enos Protein

The present study tests the hypothesis that age-dependent increases in endothelial vasodilator capacity are due to maturational increases in endothelial nitric oxide (NO) synthesis and release. Intact 4-cm carotid artery segments taken from term fetal lambs and nonpregnant adult sheep were perfused by using a closed system that enabled independent control of flow and inflow pressure and facilitated complete recovery of all NO released. Fluid shear stress induced a graded release of NO (in nmol NO·min·cm−2of luminal surface area) that was significantly greater in adult (890 ± 140) than in fetal (300 ± 40) carotid arteries at corresponding values of shear stress (5.9 ± 0.3 dyn/cm2) but was independent of inflow pressure in both age groups. These age-related differences in NO release were not attributable to corresponding differences in endothelial NO synthase (eNOS) abundance, as eNOS protein levels (in ng of eNOS/cm2of luminal surface area) were similar in adult (14 ± 2) and fetal (12 ± 1) arteries. Adult (80 ± 15) and fetal (89 ± 32) levels of eNOS mRNA (in 106copies/cm2of luminal surface area) were also similar. However, when NO release was normalized relative to the associated mass of eNOS protein to estimate eNOS-specific activity in situ, this value (in nmol NO·μg of eNOS−1·min−1) was significantly greater in adult (177 ± 44) than in fetal (97 ± 36) arteries when the endothelium was maximally activated by A-23187. Similarly, the slope of the relation between fluid shear stress and estimated eNOS-specific activity (in nmol NO·μg of eNOS−1·min−1per dyn/cm2) was also significantly greater in adult (6.8 ± 0.1) than in fetal (2.9 ± 0.1) arteries, which suggests that eNOS may be more sensitive to or more efficiently coupled to activating stimuli in adult compared with fetal arteries. We conclude that maturational increases in endothelial vasodilator capacity are attributable to age-dependent increases in NO release secondary to elevated eNOS-specific activity and involve more efficient coupling between endothelial activation and enhancement of eNOS activity in adult compared with fetal arteries.

Acid Phosphatase Activity in Vegetative Cells and Spores of Clostridium botulinum Type E

1971 ◽  
Vol 28 (11) ◽  
pp. 1817-1820 ◽  
Author(s):  
G. A. Strasdine ◽  
Joanne M. Melville
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Clostridium Botulinum ◽  
Specific Activity ◽  
Growth Media ◽  
Ph Optimum ◽  
Vegetative Cells ◽  
Botulinum Type ◽  
Clostridium Botulinum Type E

Acid phosphatase activity with a pH optimum of 5 was demonstrated in vegetative cells, spores, and germinated spores of Clostridium botulinum type E (Minnesota). The enzyme was present in the cells during all stages of growth and was insensitive to the orthophosphate concentration of the growth media. Specific activity of the enzyme increased during growth coincident with a loss in inorganic phosphate from the acid-soluble cell fraction. Magnesium or manganese was required for maximum enzyme activity. Acid phosphatase in crude spore extracts was more heat-stable than in extracts obtained from vegetative cells.

Identification of semen in stain by determination of the specific activity of l-tartrate-inhibitable acid phosphatase

1989 ◽  
Vol 102 (7) ◽  
Author(s):  
Keiji Tamaki ◽  
Kazue Fujisawa ◽  
Hiroshi Okajima ◽  
Keizo Sato ◽  
Yoshinao Katsumata
Keyword(s):  
Acid Phosphatase ◽  
Specific Activity
Sign in / Sign up

Export Citation Format

Share Document