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At least 19 recordsLinked to original sources
PubMed1985

Studies of the heterogeneity of carp liver acid phosphatases: acid phosphatase--I. Subunit structure and carbohydrate composition.

The three molecular forms of the carp liver acid phosphatase (AcPase) were shown to be dimeric proteins, two of them differing in molecular weights. An activating effect of ConA binding on the AcPases has been observed. AcPase I and AcPase II showed a mol. wt of 122,500 and of 58,884 +/- 3000 for their subunits. It is assumed that AcPase I is a sialylated derivative of AcPase II. AcPase III has a mol. wt of 93,132 and the two subunits of 46,556 +/- 4000. A homogeneous AcPase I was obtained and its carbohydrate composition is presented.

Acid Phosphatase↗
PubMed1976

Histochemical studies on the distribution of alkaline phosphatase, acid phosphatase, 5-nucleotidase and ATPase in various reproductive tissues of certain digenetic trematodes.

Out of other functions performed by vitellaria in digenetic trematodes, their role in the formation of shell globules and shell membrane of the capsule, as well as in the excretion of iron with the help of vitamin C is very important. The present histochemical work shows the localization of certain enzymes in different parts of the reproductive system of ten species of trematodes viz.: Neopronocephalus triangularis Mehra, 1932; Glossimetra orientalis Mehra, 1937; Orientodiscus lobatus Srivastava, 1938; Eumegacetes artemii Mehra, 1935; Ganeo tigrinus mehra et Negi, 1928; Encyclometra caudata Dollfus, 1928; Thapariella udaipurensis Gupta and Sharma, 1970; Paradistomoides indicum Narain et Das, 1929; Patagifer wesleyi Verma, 1936; Proalarioides tropidonotus Vidyarthi, 1937 and indicates their functional significance. The hydrolytic enzymes (alkaline phosphatase, acid phosphatase, 5-nucleotidase and ATPase) are suggestive of their involvement in the uptake of certain nutrients, glycogen and lipoprotein being very significant among others. The four enzymes could also be detected in testes, ovary, uterus, cirrus sac and egg shell. The possible functional significance of each enzyme has been discussed.

Acid Phosphatase↗
PubMed1992

[Biochemical aspects of the toxic effects of Supermethrin and the histochemical activity of alkaline phosphatase, acid phosphatase and non-specific esterase in subchronic poisoning in sheep].

Fifteen Slovak Merino sheep were included in the experiment. The animals weighing 21-28 kg were divided into three groups per five animals. In a six-week feeding experiment the animals of group I were given 50 mg supermethrin per kg live weight per day while those of group II received 200, and from week four of the experiment 300 mg supermethrin per kg live weight per day. During the experiment changes of aspartate aminotransferase (EC 2.6.1.1), alanine aminotransferase (EC 2.6.1.2), acetylcholine esterase (EC 3.1.1.7), urea und creatinine levels in blood serum were observed. Six weeks after supermethrin treatment the sheep were slaughtered and histochemical evaluation of alkaline phosphatase (EC 3.1.3.2), acid phosphatase (EC 3.1.3.1) and non-specific esterase (EC 3.1.1.1) was carried out in liver, kidney, duodenum, jejunum and ileum. In the course of the experiment changes of the enzymatic activities of aspartate aminotransferase observed in both experimental groups of sheep were similar to those seen in the control group of animals (Tab. I). As compared to the starting values, no significant changes in the activity of alanine aminotransferase were observed in group II of the experiment and in the controls. However, a significantly decreased alanine aminotransferase activity could be seen in the blood serum of sheep of group I (Tab. II). In both experimental groups of animals no significant changes in the acetylcholine esterase could be seen (Tab. III). As compared to the starting values, no significant changes were observed in creatinine levels of the control and the 1st experimental group of sheep (Tab. IV). In the sheep of the 2nd group a temporary significant decrease (p < 0.05) in creatinine levels was seen. The dynamics of urea levels was similar to starting values in all animals throughout the experiment Tab. V). In the control group of animals (Fig. 1) the high density of reaction product of alkaline phosphatase was determined in the microvilli of enterocytes of the small intestine. In the small intestine of the animals of both experimental groups, the activity of this enzyme was shown to be located in the same zone (Fig. 2). In all experimental animals in the parenchyma of the liver and kidney no significant changes could be observed. In both experimental and control animals the high activity of acid phosphatase was demonstrated to be located especially in the cytoplasma of enterocytes. The activity of non-specific esterase was located in the cytoplasma of enterocytes of the small intestine, in the intestinal crypts its activity was slight up to high.(ABSTRACT TRUNCATED AT 400 WORDS)

Acid Phosphatase↗
PubMed1975

Histochemical studies of human breast tumors: Activity of alkaline phosphatase, acid phosphatase and glucose-6-phosphate dehydrogenase.

Histochemical studies of human breast tumors were performed with particular emphasis on the activity of alkaline phosphatase (AIP), acid phosphatase (AcP) and glucose-6-phosphate dehydrogenase (G6PDH). Enzyme activities in benign and malignant lesions were compared. AIP was prominent in normal mammary epithelium, limited to the myoepithelial layer in benign tumors and was absent in cords of malignant cells. AcP activity was faintly detected in normal mammary epithelium, increased in canalicular epithelium of fibroadenomas and was marked in malignant cells. G6PDH exhibited marked activity in neoplastic epithelium and the stroma of nearly all carcinomas studied, whereas in benign tumors, G6PDH activity was strictly limited to the connective tissue. The study suggests a strong correlation between G6PDH activity and malignancy. The different results obtained by various workers in this field are critically reviewed, and discussed in the light of the results of the present study.

Acid Phosphatase↗
PubMed1992

Effects of mebendazole, albendazole, and praziquantel on alkaline phosphatase, acid phosphatase, and adenosine triphosphatase of Echinococcus granulosus cysts harbored in mice.

Mice infected with protoscoleces of Echinococcus granulosus for 12-14 months were treated ig with mebendazole (Meb) 25-50 mg.kg-1 x d-1 for 7-14 d, albendazole (Alb) 200 mg.kg-1 x d-1, cr praziquantel (Pra) 500 mg.kg-1 x d-1 for 14 d. The mice were killed 24 h after the last medication, and acid phosphatase (ACP), alkaline phosphatase (AKP), and adenosine triphosphatase (ATPase) including (Na, K, Mg)-ATPase, (Na, K)-ATPase, and (Mg)-ATPase were determined and compared with those of untreated control group. The results showed that ACP activities of cyst wall in treated groups were lower than the control group. Whereas AKP activity of cyst wall in Pra group increased markedly, this is not the case in Meb and Alb groups. Three ATPase activities of cyst wall were inhibited in both Meb and Alb groups, Meb being more potent. No apparent changes in the ATPase activities were seen in Pra group.

Acid Phosphatase↗
PubMed1977

Influence of L-thyroxine upon enzymatic activity in the renal tubular epithelium of the rat under normal conditions and in mercury-induced lesions. I. Histochemical studies of alkaline phosphatase, acid phosphatase, adenosine- tri-phosphatase and leucine-aminopeptidase.

HgC12-induced renal tubular lesions in the rat present histochemically with a transitory decrease of alkaline phosphatase, adenosinetriphosphatase (ATPase), and leucine-aminopeptidase activity. The toxic alterations of enzyme activity were more pronounced in the pars recta of the proximal tubule and in the loop of Henle, as compared with the tubulus contortus I. L-thyroxine treatment leads to an accelerated reversal of that enzymatic defect, followinga characteristic pattern, and to a differentiating increase of acid phosphatase and ATPase activity in certain parts of the normal renal tubule. The observations are discussed with reference to the specific mode of action of sublimate and l-thyroxine upon the tubular enzymes and to the well-known metabolic and functional influences of thyroid hormone on the kidney.

Acid Phosphatase↗