Gene/Protein Disease Symptom Drug Enzyme Compound
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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 structure and histochemistry of the palmar and plantar skin were studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). In this skin there exist well-developed epidermal ridges, to which are attached one or two ducts of sweat glands. A thick stratum corneum can be seen in the epidermis, while a distinct stratum lucidum cannot be isolated from the other layers. The stratum granulosum is constituted by one or three layers of cells containing keratohyalin granules. Melanin granulations are mainly concentrated in the basal cells of the epidermal ridges. Dendritic melanocytes and amelanotic melanocytes containing alkaline phosphatase are found among the epidermal cells. Glycogen, UDPG-GT and phosphorylases are mainly present in the middle and lower Malpighian cells of the epidermal ridges. Alkaline phosphatase, ATPase, alanyl amino-peptidase and leucine aminopeptidase were absent in the epidermal cells. SDH, cytochrome oxidase, MAO and a certain number of NAD-dependent dehydrogenases (LDH, ADH, MDH, alpha-GPDH, beta-OHBDH and GDH) showed a stronger reactivity in the basal cells and Malpighian layer. The NADP-dependent enzymes (G-6-PDH, 6-PGDH, cis-aconistase and ICDH) were more reactive in the upper Malpighian layer and stratum granulosum. The stratum corneum showed some acid phosphatase and nonspecific esterase reactivity. The collagenous fibers intertwined with a small number of very thin elastic ones and a larger amount of reticular fibers run almost parallel to the epidermal ridges in the papillary body. In the reticular dermis some fibers are disposed transversely to the epidermal ridges. Meissner corpuscles reactive to butyrylcholinesterase, acetylcholinesterase, nonspecific esterase and G-6-PA are disposed at regular intervals and frequently at each side of the epidermal ridges. Pacinian corpuscles were found only in the hypodermis. The eccrine sweat glands contain glycogen, UDPG-GT and phosphorylase in their secretory, ductal and myoepithelial cells. The secretory part shows a uniform reactivity for every dehydrogenase because it contains only one type of cells (clear cells). The intraepidermal segment of the ducts shows a stronger reactivity to nonspecific esterase and NADP-dependent dehydrogenases than the epithelial cells around it.
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PMID:The skin of the palms and soles of the marmosets (Callithrix jacchus and Callithrix penicillata). 82 86

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

Within the uterine glands, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the activities of G-6-PDH, 6-PGDH, and cytochrome oxidase increase within secreting cells during the 2nd half of pregnancy. The activities of the other enzymes remained almost unchanged during the period of investigation. The description of our results distinguishes between gland neck, middle, and distal part of the secretory unit, respectively. In general, the enzyme activities are similar within the middle and distal gland segments, but lower in the epithelia of the neck region. The activity of dehydrogenases was medium to intensive within the middle and distal gland segments, but only low to medium within the neck portion. Of the hydrolases, the acid phosphatase, ATPase, leucine aminopeptidase, and beta-galactosidase demonstrated an intensive activity within activity secreting cells. The enzyme activities of the gland epithelia are compared with these of the uterine surface epithelia and the histochemical results are discussed in context with their significance in histiotrophic nutrition.
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PMID:[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium]. 309 49

In porcine interareolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetylhexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, nonspecific esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that most of the enzyme activities remained almost unchanged during the period of investigation. Only G-6-PDH and 6-PGDH activities increased within the uterine epithelium and nonspecific esterase activity within uterine as well as chorionic epithelia during the 2nd half of pregnancy. Within chorionic and uterine epithelia, hydrolases but not dehydrogenases demonstrated a higher activity at the bases of chorionic villi as compared to the apices and flanks of the latter. The action and influence of the demonstrated enzymes on metabolism, energy transfer, secretory, and resorptive activities of chorionic and uterine epithelia are discussed.
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PMID:[Enzyme histochemical studies of the swine placenta. Histoptics of enzymes in interareolar placental epithelia]. 643 35