Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The histrochemistry of the adrenal glands was studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). It was impossible to demonstrate any reactivity to UDPG-GT, ADH, alanyl aminopeptidase, leucine aminopeptidase, xilitol (NAD-dependent) dehydrogenase, beta-glucuronidase and aryl-sulfatase in these glands. Total phosphorylase was found in scattered cells of the glomerulosa and adjacent outer fasciculata of one C. penicillata. The dehydrogenases (LDH, G-6-PDH,6-PGDH, NADPH2-TR,ICDH,SDH,NADH2-TR, alpha-GPDH, beta-OHBDH) as well as the hydrolases (except alkaline phosphatase, ATPase, and acetylcholinesterase) showed a stonger reactivity in the cortical part. Some hydrolases (naphthol acetate esterase, acid phosphatase) and cytochrome oxidase were less reactive in the zona glomerulosa, where the dehydrogenases were more abundant. The outer fasciculata and the reticularis also showed a strong dehydrogenase reactivity.
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PMID:Histochemical studies on the adrenal glands of the marmosets (Callithrix jacchus and Callithrix penicillata). 0 44

The histochemistry of the neural cells was studied in the submandibular ganglia of 5 Callithrix jacchus (3 males and 2 females) and 4 Callithrix penicillata (2 males and 2 females). These cells contain neutral mucopolysaccharides, nucleoproteins and lipidic materia, but are apparently devoid of glycogen. It is impossible to demonstrate in them any reactivity for UDPG-GT, phosphorylases, ATPase at pH 6.3, leucine aminopeptidase and alanyl aminopeptidas. The reaction for the other searched enzymes was as follows: weak (F-1,6-P Ald and cytochrome oxidase), weak to moderate (ADH, 6-P-GDH, ICDH, SDH, MDH, alpha-GPDH and beta-OHBDH), moderate (G-6-PDH, F-1,6-PA, LDH and GDH), moderate to strong (ATPase at pH 7.4, nonspecific esterase and acid phosphatase) and strong (G-6-PA, NADH2,-TR, NADPH2-TR, ATPase at pH 8.5 and 9.4 and alkaline phosphatase).
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PMID:Histochemical studies on the submandibular ganglia of marmosets (Callithrix jacchus and Callithrix penecillata). 14 13

The epithelial cells in the taste buds of C. jacchus and C. penicillata show a moderate amount of ribonucleic acid an a concentration of a PAS-positive diastase-resistant material at their apical part. These cells are devoid of UDPG-GT, phosphorylases, G-6-PA, alanyl aminopeptidase, leucine aminopeptidase, cholinesterase and MAO; they present a weak reaction of F-1, 6-P Ald, LDH, SDH, MDH, cytochrome oxidase, beta-OHBDH, nonspecific esterase and acid phosphatase and a stronger reaction to ADH, NADPH2-TR, ATPases, alpha-GPDH, alkaline phosphatase, 5-nucleotidase and GDH. Although some enzymes (alkaline phosphatase, 5-nucleotidase and ATPases) have an almost uniform reactivity by the several taste buds, the other ones react with a lesser intensity in the smaller uniform reactivity by the several taste buds, the other ones react with a lesser intensity in the smaller taste buds of the fungiform papillae. As a rule the apical part of the cells shows a stronger enzymatic reactivity. The taste buds of the marmosets are penetrated by acetylcholinesterase positive nerve fibers whereas the autonomic ganglia in the connective tissue contain both-acetyl and butyrylcholinesterase.
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PMID:Histochemical observations on the taste buds of the marmosets (Callithrix jacchus and Callithrix penicillata). 15 39

Histoenzymologic differences between the parotid, paramandibular and submandibular glands were studied in six Callithrix jacchus (four males and two females) and four Callithrix penicillata (three males and one female). The acinous cells of the paramandibular glands showed a stronger reactivity for the diaphorases (NADH2-TR and NADPH2-TR) and for a certain group of enzymes of the carbohydrate metabolism (F-1-6P Ald, LDH, ADH, G-6-PDH and 6-PGDH), lipid metabolism (alpha-GPDH, beta-OHBDH, alkaline phosphatase and acid phosphatase), protein metabolism (alanyl aminopeptidase, leucine aminopeptidase and GDH) and respiratory chain (cris-aconitase and ICDH). The nonspecific esterase was more reactive in the basal part of of the mucous cells of the submandibular glands. Conversely, some enzymes of the respiratory chain (SDH, cytochrome oxidase and ATPases) showed a stronger reactivity in the serous cells of the parotid and submandibular glands. The paramandibular glands exhibited a lesser autonomic innervation than the parotid and submandibular.
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PMID:Histochemical differences between the major salivary glands of the marmosets (Callithrix jacchus and Callithrix penicillata). 82 38

The enzyme pattern of 13 cases of malignant fibrous histiocytoma (MFH) and 11 cases of myxofibrosarcoma (MFS), a malignant myxomatous soft tissue tumor of fibroblastic histiocytic origin, has been studied. 6 of the 13 MFHs were analyzed enzyme histochemically at the light microscopic level and 7 on the ultrastructural level; of the 11 MFSs 9 were analyzed enzyme histochemically at the light microscopic level and 2 on the ultrastructural level. Differences were observed in the subjectively estimated enzyme activity between low grade MFS and high grade MFS and MFH, and also between histiocyte-like and fibroblast-like tumor cells. Generally a strong reaction of oxidoreductase enzymes (NADH2-diaphorase, NADPH2-diaphorase, glucose-6-phosphate dehydrogenase) and hydrolytic enzymes (acid phosphatase and leucine aminopeptidase) was found in the high grade tumors and was usually higher in the histiocyte-like than in the fibroblast-like cells. Ultrastructurally acid phosphatase occurred predominantly in primary and secondary lysosomes and Golgi zones of the histiocyte-like cells. A strong reaction of alkaline phosphatase was found light microscopically in 2 of 5 MFHs and 5 of 9 MFSs. Ultrastructurally alkaline phosphatase was located along the cytoplasmic membrane of predominantly fibroblast-like cells in 3 of 7 MFHs and 1 of 2 MFSs. The results agree with the concept of two main cell types in MFH and MFS, fibroblasts and histiocytes.
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PMID:Enzyme histochemistry of malignant fibroblastic histiocytic tumors. A light and electron microscopic analysis. 608 56

Oxygen and glucose consumption and lactate production of the peritoneal membrane and intra-abdominal adhesions were measured in rats after a single intra-peritoneal colloidal silica injection. Enzyme histochemical studies were made of lactate dehydrogenase, succinate dehydrogenase, NADH2-diaphorase, NADPH2-diaphorase, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, acid phosphatase, leucylaminopeptidase and alkaline phosphatase in the peritoneal membrane. Anaerobic glycolysis comprises 47% of the total glucose consumption in the the normal peritoneum. Glucose consumption and lactate production of the peritoneal membrane increased sharply in the early phase of silica-induced peritonitis and stayed at a high level for a week indicating an enhanced anerobic metabolism. Oxygen and aerobic glucose consumption increased more slowly than anaerobic glucose consumption and reached their maxima 1 week after silica injection, indicating that the rate of aerobic metabolism is also higher in chemical peritonitis than in the controls. On the other hand, glucose consumption and lactate production increased in a parallel fashion in adhesions and in the peritoneum in the early phase of peritonitis. However, the maximum and later levels were less in adhesions than in the peritoneum. In the enzyme histochemical study high activities of enzymes indicating anaerobic energy metabolism and metabolism via the pentose phosphate shunt were seen in cells of the peritoneal membrane during the early phase of peritonitis. No activity was identified in enzymes indicating aerobic energy metabolism and increased catabolism before the end of the first week.
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PMID:Energy metabolism of the peritoneal membrane in silica-induced peritonitis. A biochemical and enzyme histochemical study. 625 64

Five min after administration of a single, i.p. dose of ammonium metavanadate (5 mg/kg), in rats, liver enzyme activities were measured. Microsomal mixed-function oxidases (except for aminopyrine N-demethylase), glucose-6-phosphatase and alkaline phosphatase were inhibited but lactate, malate, and glycerophosphate dehydrogenases as well as microsomal NADPH2-dependent cytochrome c reductase were unchanged.
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PMID:Effects of ammonium metavanadate on rat liver enzymes. 660 66