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.

EFFECTS OF CASTRATION AND ANDROGEN REPLACEMENT ON ACID PHOSPHATASE ACTIVITY IN THE ADULT RAT PROSTATE GLAND

1978 ◽  
Vol 77 (3) ◽  
pp. 301-NP ◽  
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 ◽  
Prostate Gland ◽  
Intraperitoneal Administration ◽  
Male Rats ◽  
Normal Value ◽  
Secretory Acid Phosphatase

Acid phosphatase (EC 3.1.3.2) activity was examined for its possible utilization as a biochemical marker for the profound changes that occur in the prostate gland after castration. Tissue filtrates were prepared from the prostate glands of mature male rats at various times after castration. The acid phosphatase activity was characterized by polyacrylamide gel electrophoresis and the percentage inhibition in the presence of tartrate. Prostatic acid phosphatase from mature rats has been shown to have two bands of activity, a lysosomal acid phosphatase and a secretory acid phosphatase. After castration, there was a loss of the secretory acid phosphatase from gel electrophoresis patterns by day 5 and a corresponding rise in the percentage inhibition by tartrate from the normal value of 43·2% to a maximum of 55·4% on day 7. Between days 7 and 15 there was a linear decrease in the percentage inhibition by tartrate, but after day 15 the value did not change significantly from 31·1% After castration, the specific activity of the uninhibited enzyme increased from a normal basal level of 2·16 μmol h−1 mg protein−1 to a maximum on day 7 of 8·10 μmol h−1 mg protein−1. After this time, the specific activity decreased slowly until it reached a normal level on day 21. Intraperitoneal administration of testosterone, 5α-dihydrotestosterone or 5α-androstane-3α,17β-diol at a dose of 2 mg/day and starting immediately after castration prevented the changes in percentage inhibition by tartrate and the loss of the secretory band of acid phosphatase. Administration of these androgens from day 7 after castration led to a decrease in the percentage inhibition from 50·1% to a minimum of 31·5% before the level returned to the normal value found in the mature rat. The secretory band of acid phosphatase, which was not present in gels at day 7, reappeared after 8–11 days of treatment with androgens. Of the androgens used,5α- androstane-3α,17β-diol was the most potent.

scholarly journals New form of acid phosphatase during lysosome biogenesis

1981 ◽  
Vol 198 (1) ◽  
pp. 9-15 ◽  
Author(s):  
G R Rao ◽  
H N Aithal ◽  
F G Toback ◽  
G S Getz
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Lysosomal Enzyme ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Deficient Diet ◽  
Lysosomal Fraction ◽  
K Depletion

Lysosome formation was induced in cells of the renal medulla by feeding rats on a K+-deficient diet. The role of the endoplasmic reticulum in the production of acid phosphatase, a typical lysosomal enzyme, was examined. Lysosomal and microsomal fractions were prepared for study by differential centrifugation of homogenates of renal papilla and inner stripe of red medulla. Acid phosphatase activity in the microsomal fraction was distinguished from the activity in the lysosomal fraction in normal tissue by differences in pH optima, tartrate inhibition, distribution of multiple forms after polyacrylamide-gel electrophoresis and detergent-sensitivity. During progressive K+ depletion, acid phosphatase activity in both microsomal and lysosomal fractions of the tissue increased 3-fold. In the lysosomes, K+ depletion was associated with the appearance of a new band of acid phosphatase. The neuraminidase-sensitivity of this band on polyacrylamide-gel electrophoresis indicated that the enzyme protein had been modified by the addition of sialic acid residues. K+ depletion also altered the lysosomal enzyme so that thiol compounds were able to stimulate its activity.

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.

GENETIC STUDIES OF ISOZYMES IN NEUROSPORA. I. A STUDY OF EIGHT SPECIES

1971 ◽  
Vol 13 (2) ◽  
pp. 298-305 ◽  
Author(s):  
M. Mohan Reddy ◽  
S. F. H. Threlkeld
Keyword(s):  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Starch Gel Electrophoresis ◽  
Acid Phosphatases ◽  
Genetic Studies ◽  
Starch Gel

Mycelial extracts of 34 strains representing eight species of the genus Neurospora were subjected to acrylamide and starch gel electrophoresis to detect sites of esterase, lactate dehydrogenase, amylase, peroxidase, and acid phosphatase activity. Nine isozymes of esterases, four isozymes of lactate dehyrogenases, three isozymes of peroxidases, and two isozymes of acid phosphatases were detected on the gels for the species. The application of zymograms as a biochemical means to characterize species is discussed.

scholarly journals Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas

1989 ◽  
Vol 261 (2) ◽  
pp. 601-609 ◽  
Author(s):  
A R Hayman ◽  
M J Warburton ◽  
J A S Pringle ◽  
B Coles ◽  
T J Chambers
Keyword(s):  
Acid Phosphatase ◽  
Gel Electrophoresis ◽  
Biochemical Characterization ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Tartrate Resistant Acid Phosphatase ◽  
Bovine Bone ◽  
Ph Optimum ◽  
Original Tumour

Tartrate-resistant acid phosphatase is one of the major enzymes produced and secreted by osteoclasts. To obtain sufficient enzyme for biochemical characterization, we have purified this enzyme from human osteoclastomas by sequential chromatography on SP-Sephadex, CM-Sephadex, hydroxylapatite, Sephadex G-150 and concanavalin A-Sepharose. The purification over the original tumour extract was about 2000-fold, with a yield of 10%. The enzyme appeared to be homogeneous when assessed by SDS/polyacrylamide-gel electrophoresis. Both gel filtration and SDS/polyacrylamide-gel electrophoresis indicated an Mr of about 30,000. The reduced and alkylated enzyme consists of two subunits with Mrs of 15,000 and 17,500. The N-terminal amino acid sequence of both subunits indicates that there is a high degree of identity between the osteoclastoma enzyme and similar enzymes purified from spleen and uterus. Using 4-methylumbelliferyl phosphate as substrate, the specific activity of the purified enzyme was 387 units.mg-1, and the Km was 284 microns. The pH optimum was 5.7. Unlike similar enzymes purified from human and bovine bone, osteoclastoma acid phosphatase is not activated by reducing agents (2-mercaptoethanol or ascorbic acid). The enzyme contains 4.8 mol of Fe2+/3+, 0.3 mol of Mn2+ and 1.7 mol of Mg2+ per mol of enzyme. Although the enzyme loses 50% of its activity in the presence of EDTA, it is not inhibited by the iron chelator 1,10-phenanthroline. However, the enzyme is activated to a small extent by Mn2+ and Mg2+. Using a variety of substrates and inhibitors, we demonstrate that there are differences between the osteoclastoma acid phosphatase and the enzyme purified from other sources.

Intraspecific genetic variation of acid phosphatase activity in monokaryotic and dikaryotic populations of the ectomycorrhizal fungus Hebeloma cylindrosporum

1991 ◽  
Vol 69 (4) ◽  
pp. 808-813 ◽  
Author(s):  
J. P. Meysselle ◽  
G. Gay ◽  
J. C. Debaud
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Specific Activity ◽  
Intraspecific Variability ◽  
Ectomycorrhizal Fungus ◽  
Hebeloma Cylindrosporum ◽  
Single Strain ◽  
Wild Strains

Intraspecific variability of acid phosphatase activity and mycelial growth of the ectomycorrhizal fungus Hebeloma cylindrosporum Romagnesi was examined because of the role of this enzyme activity in the phosphate nutrition of the fungus and consequently of mycorrhizal host plants. Interstrain variation was studied with 11 wild strains, and intrastrain variability was studied with 20 sib-monokaryons and 50 reconstituted dikaryons, progeny of the HC1 fruiting strain. The range of variation of acid phosphatase activity among wild dikaryotic mycelia was the same as that among sib-monokaryons or dikaryons belonging to the progeny of a single strain. The total phosphatase activity of the wild strains ranged from 5.70 to 96.0 total milliunits (TmU). It ranged from 11.1 to 120.5 TmU within sib-monokaryons and from 34.2 to 178.1 TmU for reconstituted dikaryons. Specific phosphatase activity of wild dikaryons ranged from 48.5 international milliunits (ImU) to 675.6 ImU, whereas the ranges of variation among sib-monokaryons and reconstituted dikaryons were, respectively, 85.3–791.0 and 270.7–816.1 ImU. On average, sib monokaryons and reconstituted dikaryons had lower activity than their parental dikaryon. However, four reconstituted dikaryons had a higher specific activity than the original dikaryon HC1. The growth of the studied mycelia also varied, but in a narrower range (from 97.1 to 151.6 μg protein per culture for wild dikaryons, from 130.1 to 199.1 μg for sib-monokaryons, and from 160.6 to 275.9 μg for reconstituted dikaryons). No correlation could be detected between specific acid phosphatase activity and growth rate in pure culture within the different monokaryotic or dikaryotic populations studied. These results demonstrate the possibility of obtaining, by intrastrain crossings, mycelia having higher phosphatase activity than the parental wild strains. The characteristics of the different mycelia are discussed in relation to a selection program and their putative spatial distribution in natural conditions. Key words: acid phosphatase, ectomycorrhizal fungus, intraspecific variation, monokaryon, dikaryon, Hebeloma cylindrosporum.

scholarly journals ACID PHOSPHATASE ISOENZYME IN HUMAN LEUKOCYTES IN NORMAL AND PATHOLOGIC CONDITIONS

1970 ◽  
Vol 18 (7) ◽  
pp. 473-481 ◽  
Author(s):  
C. Y. LI ◽  
L. T. YAM ◽  
K. W. LAM
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Lymphocytic Leukemia ◽  
Total Acid ◽  
Chronic Granulocytic Leukemia ◽  
Human Leukocytes ◽  
Number Of Patients ◽  
Granulocytic Leukemia

Acid phosphatase in human leukocytes was examined in a large number of patients with a variety of hematologic diseases. In chronic lymphocytic leukemia the total leukocyte acid phosphatase activity was markedly decreased. This was due to the drastic increase of enzyme-poor leukemic lymphocytes and the concomitant decrease of enzyme-rich monocytes and neutrophils. Further examination by disc gel electrophoresis revealed that the leukocytes in this disease contained only one of the five acid phosphatase isoenzymes present in a normal leukocyte preparation. Total acid phosphatase activity was not significantly altered in other hematologic disorders, yet different ratios of the isoenzymes shown by disc gel electrophoresis were observed in Hodgkin's disease, chronic granulocytic leukemia, acute granulocytic leukemia, infectious mononucleosis and leukemic reticuloendotheliosis.

Sign in / Sign up

Export Citation Format

Share Document