Acid phosphatase activity demonstrated in the nematodes, Dirofilaria immitis and Angiostrongylus cantonensis with special reference to the characters and distribution

Parasitology ◽  
1980 ◽  
Vol 80 (1) ◽  
pp. 23-38 ◽  
Author(s):  
Jun Maki ◽  
Toshio Yanagisawa
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Dirofilaria Immitis ◽  
Body Wall ◽  
Dry Weight ◽  
The Body ◽  
Angiostrongylus Cantonensis ◽  
Total Acid ◽  
Noticeable Effect

SummaryAcid phosphatase activity was demonstrated in the intact blood nematodes, Dirofilaria immitis and Angiostrongylus cantonensis. Biochemical studies on acid phosphatase, using intact females and whole worm, body-wall and visceral homogenates were undertaken to clarify the characteristics and the distribution of the enzyme. In D. immitis, high acid phosphatase activity was observed at pH 3·8–5·8 and in A. cantonensis, at pH 4·5–6·0. Molybdate, fluoride, copper and zinc ions and L(+)-tartrate were effective inhibitors of the enzymes of both parasites while cobalt and magnesium ions and D(−)-tartrate had no noticeable effect on the activity. When the effect of substrate concentration on the phosphatase activity was studied, kinetic curves of Michaelis–Menten type were obtained with the 2 species of intact worms as well as their homogenates. The reproductive organs and body wall of D. immitis showed high total acid phosphatase activity. In A. cantonensis, the majority of the enzyme was localized in the body wall. The activity of intact A. cantonensis expressed as μg Pi/h/mg dry weight decreased with increase in mean worm weight. The characteristics of the acid phosphatase of the 2 nematodes are compared with those of other parasitic helminths and of acid phosphatase of mammalian origin. The localization of the phosphatase responsible for the hydrolysis of the external substrate has been discussed for D. immitis and A. cantonensis based on results of the kinetics and distribution of the enzyme.

A comparison of the sites of acid phosphatase activity in an adult filaria, Setaria sp. and in some gastro -intestinal nematodes

Parasitology ◽  
1980 ◽  
Vol 81 (3) ◽  
pp. 603-608 ◽  
Author(s):  
Jun Maki ◽  
Toshio Yanagisawa
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Alimentary Canal ◽  
Body Wall ◽  
The Body ◽  
Luminal Surface ◽  
Toxocara Cati ◽  
Similar Activity ◽  
Very High

SUMMARYThe histochemical localization of acid phosphatase in an adult filaria, Setaria sp. obtained from the peritoneal cavity of a cow was closely examined and compared with that of adult nematodes parasitic in the host alimentary canal; special attention was paid to the intestine and body wall of the parasites. Setaria sp. was found to show high acid phosphatase activity in the interchordal hypodermis of the body wall and uterine microfilariae, and similar activity is suspected to occur in the cuticle. The intestine of this nematode exhibited very low, if any, activity. In contrast, nematodes parasitic on the alimentary canal, such as Toxocara cati, T. canis, Physaloptera sp. and Ancylostoma caninum, showed no activity in the body wall and very high activity in the luminal surface of their intestine. The possible function of the abundant acid phosphatase in the body wall of this filaria is discussed.

ACID PHOSPHATASE ACTIVITY IN VIABLE AND REGRESSING RAT CORPORA LUTEA

1970 ◽  
Vol 47 (2) ◽  
pp. 167-176 ◽  
Author(s):  
JEANNE A. SMITH ◽  
H. B. WAYNFORTH
Keyword(s):  
Acid Phosphatase ◽  
Corpus Luteum ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Enzymic Activity ◽  
Corpora Lutea ◽  
Cellular Composition ◽  
Total Acid ◽  
Progesterone Secretion ◽  
Experimentally Induced

SUMMARY Free and total acid phosphatase activity has been measured in individual corpora lutea from rat ovaries in various reproductive states (both natural and experimentally induced). Significant changes both in weight and enzymic activity were found, and an attempt has been made to correlate these with the growth and regression of the corpora lutea. A possible connexion between acid phosphatase activity, progesterone secretion and/or cellular composition of the corpus luteum is suggested.

Phytase and acid phosphatase activities in extracts from roots of temperate pasture grass and legume seedlings

1999 ◽  
Vol 26 (8) ◽  
pp. 801 ◽  
Author(s):  
Julie E. Hayes ◽  
Alan E. Richardson ◽  
Richard J. Simpson
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Trifolium Subterraneum ◽  
Phytase Activity ◽  
Sand Culture ◽  
Total Acid ◽  
Pasture Grass ◽  
P Deficiency ◽  
Phosphatase Activities

Phytase and acid phosphatase activities were measured in extracts from roots of 14- to 22- day old seedlings of a range of temperate pasture species that were grown aseptically in sand culture. Phytase activity from roots of phosphorus- (P-)-deficient Trifolium subterraneum L. was characterised. Activity was enhanced by 40% when extracts were passed through Sephadex G-25, and increased by a further 20–30% with the addition of either 1 mМ EDTA or 5 mМ cysteine to assay solutions. The optimum temperature for phytase activity was 50°C and the optimum pH was 5.3. When compared with phosphatase activity measured in the roots of T. subterraneum, phytase activity exhibited narrower pH and temperature optima, and was also more strongly inhibited by Co2+, Zn2+ and AsO42− ions. Significantly, for the five pasture species examined, phytase activity was less than 5% of the total acid phosphatase activity in extracts of plant roots. Measured phytase activity ranged between 0.13 and 1.7 nkat g–1 root fresh wt and was enhanced under P-deficient relative to P-sufficient growth conditions in all of the pasture species with the exception of Trifolium repens L., for which the Km constant for activity was 50% lower in P-deficient plants. When expressed on a root fresh wt basis, increases in phytase activity of ~1.25-fold were observed for extracts from T. subterraneum and Medicago polymorpha L., and of up to 3.3-fold for Danthonia richardsonii A.B. Cashmore and Phalaris aquatica L. Increases in acid phosphatase activity with P deficiency were less evident. Between 3.1% and 4.3% only of the total phytase activity measured in root extracts was eluted from intact roots into 0.1 М NaCl.

ACID PHOSPHATASE ACTIVITY IN THE RAT NEUROHYPOPHYSIS DURING INCREASED LEVELS OF GONADOTROPHIC HORMONES, IN DIABETES INSIPIDUS (BRATTLEBORO STRAIN) AND AFTER WATER LOADING

1976 ◽  
Vol 81 (3) ◽  
pp. 697-706 ◽  
Author(s):  
G. J. Boer ◽  
F. W. van Leeuwen ◽  
D. F. Swaab ◽  
J. W. L. Nolten
Keyword(s):  
Acid Phosphatase ◽  
Diabetes Insipidus ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Dry Weight ◽  
Neurosecretory Material ◽  
Water Metabolism ◽  
Water Loading ◽  
Hormone Levels ◽  
Stimulation Of

ABSTRACT The acid phosphatase activity of the rat neurohypophysis was measured during increased gonadotrophic hormone levels, in diabetes insipidus (DI) (Brattleboro strain) and after water loading, i. e. conditions that interfere with the function of the hypothalamo-neurohypophyseal system (HNS). In addition determinations of tissue protein, lipid and DNA and of water metabolism were performed. Neurohypophyseal acid phosphatase activity expressed on a dry weight basis increased under all conditions. For gonadectomized females, Brattleboro rats and water loaded males an increased water metabolism was observed. The increased acid phosphatase activity is interpreted as being related to disposal of release residues during stimulation of the HNS (increased gonadotrophic hormone levels and DI) and to disposal of neurosecretory material during inhibition (water loading).

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.

Prostatic acid phosphatase assay with self-indicating substrate 2,6-dichloro-4-acetylphenyl phosphate

1995 ◽  
Vol 41 (2) ◽  
pp. 200-203 ◽  
Author(s):  
S Osawa ◽  
S Iida ◽  
H Yonemitsu ◽  
K Kuroiwa ◽  
K Katayama ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Dynamic Range ◽  
Kinetic Method ◽  
High Specificity ◽  
Prostatic Acid Phosphatase ◽  
Molar Absorptivity ◽  
Total Acid ◽  
Phosphatase Assay

Abstract We characterized six self-indicating substrates, synthesized as the derivative compounds of acetylphenyl phosphate, for serum prostatic acid phosphatase (PAP) activity. One of the substrates, 2,6-dichloro-4-acetylphenyl phosphate (DCAPP), is superior to others in terms of stability, affinity, and low Km for PAP. The hydrolyzed product, 2,6-dichloro-4-acetylphenol (DCAP), has a maximum absorption at 334.2 nm, a pKa of 4.15, and a molar absorptivity at 340 nm of 21,490 L.mol-1.cm-1 in citrate-HCl buffer, pH 5.4. PAP activity was assessed by subtracting tartaric acid-inhibited acid phosphatase activity from total acid phosphatase activity. Our assay system involving DCAPP is a unique kinetic method that shows good reproducibility, wide analytical dynamic range, and high specificity for PAP. Moreover, it is easily adaptable to automated analyzers because the product, DCAP, can be monitored at 340 nm.

ACTIVITY OF ACID PHOSPHATASE IN THE SERUM OF NORMAL INFANTS AND CHILDREN

PEDIATRICS ◽  
1960 ◽  
Vol 26 (2) ◽  
pp. 281-284
Author(s):  
Zvi Laron ◽  
Batia Epstein-Halberstadt
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Tartaric Acid ◽  
Acid Phosphatase Activity ◽  
Normal Values ◽  
Newborn Infants ◽  
Infants And Children ◽  
Total Acid ◽  
Medium Level ◽  
Inhibited Acid

Normal values for activity of acid phosphatase in the serum of infants and children are presented. The total acid phosphatase activity is high in the serum of newborn infants, declines slightly during the first 2 weeks of life, remains at a medium level up to the age of 13 and then further declines until it reaches a low level found in adults, around the age of 17 years. The activity of tartaric acid-inhibited acid phosphatase in serum is similar in all ages. A disparity between acid phosphatase activity in the serum of mothers and their infants is described.

Sign in / Sign up

Export Citation Format

Share Document