Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.9 (glucose-6-phosphatase)
 3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The dermal cells in grey, xanthic, and white goldfish integuments were cytochemically characterized for the following enzymatic activities: tyrosinase, DOPA-oxidase, cytochrome oxidase, monoamine oxidase, peroxidase, non-specific esterase, cholinesterase, NAD-diaphorase, NADP-diaphorase, aryl sulfatase, nucleotide phosphodiesterase, beta-glucuronidase, acid phosphatase, alkaline phosphatase, adenosine triphosphatase, thiamine pyrophosphatase, glucose-6-phosphatase, aldolase, as well as succinate, malate, isocitrate, glutamate, glucose-6-phosphate, 6-phosphogluconate, alpha-glycerophosphate, alcohol, lactate, and beta-hydroxybutyrate dehydrogenases. It was found that the epidermis was a significant barrier to the access of cytochemical reaction substrates. Removal of the epidermal barrier provided dermal cell localizations of enzymatic activities which were reproducible. Further, alterations in reaction times and temperatures from the mammalian methodology provided conditions fe various integumental cells were compared for possible interrelationships. The basic foundations for future work with the dermis of poikilothermic vertebrates on an experimental basis were established. In addition, a previously undescribed non-pigmented dermal cell, the "x"-cell, was found to have enzymatic characteristics similar to both melanophores and lipophores. The "x"-cell may be the common precursor of both types of pigment cells.
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PMID:Cytochemical characterization of goldfish (Carassius auratus L.) dermis with special reference to the pigment cells. 82 86

Glycogen synthase, glycogen phosphorylase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and glucose-6-phosphatase were determined for the first time in the necessary lobes of Lachi from late embryonic chicks. The activities of these enzymes were compared with those found in other glycogen-metabolizing tissues, specifically the glycogen body, liver, and skeletal muscle, obtained from the same embryos. The data show that, as in the glycogen body, the accessory lobes of Lachi lack glucose-6-phosphatase, but contain relatively high activity levels of glycogen synthase I, total and active glycogen phosphorylase, and the dehydrogenases of glucose-6-phosphate and 6-phosphogluconate. The percent of glycogen synthase I activity in the Lachi lobes is from two- to 20-fold greater than observed in the glycogen body, liver, or muscle, whereas the percent of glycogen phosphorylase a activity is comparable to that of the liver, but greater than that in the glycogen body or muscle. The activity of each dehydrogenase of the pentose phosphate cycle in the Lachi lobes is similar to that noted in the glycogen body, but is over two- or fivefold greater than that activity found in muscle or liver. Our data, together with other recent evidence, suggest that the role of glycogen in these functionally enigmatic tissues may be to support the precocious process of myelin synthesis in the developing bird, as well as possibly to provide alternate sources of energy for the avian central nervous system.
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PMID:Glycogen metabolism in the developing accessory lobes of Lachi in the nerve cord of the chick: metabolic correlations with the avian glycogen body. 678 75

The existence of glucose-6-phosphate transport across the liver microsomal membrane is still controversial. In this paper, we show that S3483, a chlorogenic acid derivative known to inhibit glucose-6-phosphatase in intact microsomes, caused the intravesicular accumulation of glucose-6-phosphate when the latter was produced by glucose-6-phosphatase from glucose and carbamoyl-phosphate. S3483 also inhibited the conversion of glucose-6-phosphate to 6-phosphogluconate occurring inside microsomes in the presence of electron acceptors (NADP or metyrapone). These data indicate that liver microsomal membranes contain a reversible glucose-6-phosphate transporter, which furnishes substrate not only to glucose-6-phosphatase, but also to hexose-6-phosphate dehydrogenase.
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PMID:Evidence for glucose-6-phosphate transport in rat liver microsomes. 1206 48