Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q8NEX9 (reductase)
 26,410 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Subcutaneous adipose tissue was obtained from fetuses removed from pregnant obese (Ossabaw) and lean (crossbred) sows at three stages of gestation (70, 90, and 110 days). Histochemical analysis for nucleo-side phosphatase (NPase), alkaline phosphatase (APase), and NADH tetrazoleum reductase (NADH-TR) was conducted on fresh-frozen cryostat sections. Age- associated changes in NPase and NADH-TR reactions in the arteriolar system were correlated with the morphological development of the medial layer of arterioles and arteries. For instance, a strong NPase reaction in small arterioles was associated temporally with the assumption of a normal smooth muscle cell morphology and arrangement in the medial layer. In the youngest fetuses, strong NADH-TR reactions were only evident in small and presumptive arterioles and venules (associated with fat cells). Little NADH-TR reactivity was evident in larger arterioles and venules in 70-day tissue. Arteries and large arterioles were distinguished from veins and venules (strong reactions vs. weak reactions) with NADH-TR and NPase reactions in the oldest fetuses. In the younger fetuses, the NPase distinction (arterioles vs. veinules) was obvious before NADH-TR distinction. Small adipocyte-associated vessels were APase positive in the youngest fetuses, but APase reactivity was limited to short segments of vessel between arterioles and capillaries in the oldest fetuses. With the following exceptions, all the above observations were independent of fetal strain. In obese fetuses (110 day) small venules and small arterioles were equally reactive for NPase activity. Capillaries in obese fetuses (110 day) were NADH-TR reactive, whereas no activity was evident in capillaries from lean fetuses (110 day).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Differentiation of blood vessels in the adipose tissue of lean and obese fetal pigs, studied by differential enzyme histochemistry. 299 39

We have developed a method for isolation of plasma membranes from rabbit endometrium, with high yield and purification. Endometrial homogenates are precipitated with calcium chloride and the resulting supernatant is fractionated by centrifugation in a self-forming gradient of 20% Percoll. Before fractionation, the intact luminal epithelial surface was labelled with 125I-labelled soyabean agglutinin. Between buoyant densities of 1.015 and 1.017 g/ml, a discrete peak of surface label was obtained, which coincided with activities for 5'-nucleotidase and alkaline phosphatase, enzyme markers for the plasma membrane. This peak was well separated from the majority of cellular protein, and from marker enzyme activities for mitochondria and microsomes (NADH cytochrome C reductase) and lysosomes (acid phosphatase). Electron microscopy of the purified membranes showed membrane sheets and vesicles free from other cellular organelles. Analysis of detergent-soluble membrane proteins, fractionated by concanavalin A-affinity chromatography, revealed differences in the protein pattern of membranes from uteri of rabbits receptive (Day 6 of pregnancy) and non-receptive (Day 3) for implantation. The method will be useful for generation of immunological and affinity probes for surface antigens involved in ovoimplantation.
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PMID:Purification of rabbit endometrial plasma membranes from receptive and non-receptive uteri. 299 83

The ribonucleoside triphosphate reductase of Lactobacillus leichmannii converts the substrate analogue 2'-chloro-2'-deoxyuridine 5'-triphosphate (ClUTP) into a mixture of 2'-deoxyuridine triphosphate (dUTP) and the unstable product 3'-keto-2'-deoxyuridine triphosphate (3'-keto-dUTP). This ketone can be trapped by reduction with NaBH4, producing a 4:1 mixture of xylo-dUTP and dUTP. When [3'-3H]ClUTP is treated with enzyme in the presence of NaBH4, the isomeric deoxyuridines isolated after alkaline phosphatase treatment retained 15% of the 3H in ClUTP. Degradation of these isomeric nucleosides has established the location of the 3H in 3'-keto-dUTP as predominantly 2'(S). The xylo-dU had 98.6% of its label at the 2'(S) position and 1.5% at 2'(R). The isolated dU had 89.6% of its label at 2'(S) and 1.4% at 2'(R), with the remaining 9% label inferred to be at the 3'-carbon, this resulting from the direct enzymic production of dUTP. These results are consistent with enzymic production of a 1:1000 mixture of dUTP and 3'-keto-dUTP, where the 3'-hydrogen of ClUTP is retained at 3' during production of dUTP and is transferred to 2'(S) during production of 3'-keto-dUTP. The implications of these results and the unique role of the cofactor adenosylcobalamin (Ashley et al., 1986) are discussed in terms of reductase being a model for the B12-dependent rearrangement reactions.
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PMID:Inactivation of the ribonucleoside triphosphate reductase from Lactobacillus leichmannii by 2'-chloro-2'-deoxyuridine 5'-triphosphate: a 3'-2' hydrogen transfer during the formation of 3'-keto-2'-deoxyuridine 5'-triphosphate. 306 62

Treatment with alkaline phosphatase of hepatic microsomes prepared from rabbit, rat, and mouse caused a marked decrease of their specific monooxygenase activity (7-ethoxycoumarin-deethylation). This decrease occurred without a significant change in the microsomal content of cytochrome P-450, but with an equally marked decrease of NADPH-cytochrome P-450 reductase (cytochrome c reduction). Thus the phosphatase effect on monooxygenase is mainly due to the inactivation of the reductase.
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PMID:Phosphatase affects microsomal monooxygenase mainly via reductase. 309 91

Incubation of rabbit liver microsomes with alkaline phosphatase resulted in a marked decrease of NADPH-dependent monooxygenase activities. This decrease was found to be correlated with the decrease of NADPH-cytochrome c reductase activity catalyzed by NADPH-cytochrome P-450 reductase. Neither the content of cytochrome P-450, as determined from its CO difference spectrum, nor the peroxide-supported demethylase activity catalyzed by cytochrome P-450 alone was affected by the phosphatase treatment. NADH-cytochrome b5 reductase and cytochrome b5 were not affected by the phosphatase either. NADPH-cytochrome P-450 reductase purified from rabbit liver microsomes lost its NADPH-dependent cytochrome c reductase activity upon incubation with phosphatase in a way similar to that of microsome-bound reductase. Flavin analysis showed that the phosphatase treatment caused a decrease of FMN with concomitant appearance of riboflavin. Alkaline phosphatase, therefore, inactivates the reductase by attacking its FMN, and the inactivation of the reductase, in turn, leads to a decrease of the microsomal monooxygenase activities.
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PMID:The effects of phosphatase on the components of the cytochrome P-450-dependent microsomal monooxygenase. 310 84

Enzyme profiles of oral Treponema species were determined by using RapID-ANA (Innovative Diagnostic System, Atlanta, Ga.), a 4-h test system which detects 18 enzymatic reactions, including aminopeptidases and glycosidases. Seventy-two clinical isolates of Treponema denticola, four reference strains of T. denticola (ATCC 35404, ATCC 35405, ATCC 35520, and ATCC 33521), one strain of T. vincentii (ATCC 35580), and two strains of T. socranskii subspecies (T. socranskii subsp. buccale ATCC 35534 and T. socranskii subsp. socranskii ATCC 35536) were used in this study. All T. denticola strains produced indole and a variety of aminopeptidases and glycosidases. These organisms could be differentiated into two groups on the basis of tetrazolium reductase and serine, phenylalanine, and glycine aminopeptidase activities. T. vincentii produced N-acetylglucosaminidase and arginine aminopeptidase, which facilitated the differentiation of this organism from T. socranskii subspecies and the T. denticola group. T. socranskii subspecies gave positive reactions for alkaline phosphatase only. These findings suggest that the RapID-ANA system is useful for enzymatic characterization and differentiation of oral spirochetes.
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PMID:Enzyme profiles of oral spirochetes in RapID-ANA system. 318 13

In alimentary deficiency of vitamin K in rats, accompanied by an increase in the prothrombin time by 30%, activity of kidney creatine kinase and of blood serum alkaline phosphatase was unaltered, while the activity of alkaline phosphatase in small intestinal mucose was decreased by 20% and that of creatine kinase from skeletal muscles--by 10%. In vitamin K-deprived animals the rate of coupling between respiration and mitochondrial phosphorylation was decreased, which might be due to alteration in the NADH-dehydrogenase complex. Menadion reductase activity and cyanide-resistant respiration of mitochondria were unaltered in presence of menadion. Palmitic acid effectively activated of mitochondrial respiration in vitamin K-deprived animals (contrary to the control rats). This effect appears to occur as a result of structural alterations in mitochondria depending on vitamin K level in the organelles.
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PMID:[The effect of vitamin K deficiency in rats on various enzyme systems participating in energy metabolism]. 319 31

The histologic and histochemical staining characteristics of the triceps brachii (long head), extensor carpi radialis, gluteus medius, vastus lateralis, biceps femoris, semimembranosus, semitendinosus, and extensor digitorum longus muscles of 8 Thoroughbreds, 2 Quarter Horses, 1 Arabian, 1 Paso Fino, and 1 Shetland Pony are described. Muscle fiber morphology, staining distribution and intensity, amount of IM connective tissue, number of IM blood vessels and IM nerves, calcium-activated adenosine triphosphatase activity (CaATPase), percentage of fibertype population, percentage of relative fibertype area, mean fiber diameter, nonspecific esterase activity, alkaline phosphatase activity, and acid phosphatase activity were evaluated, using 10 common histochemical and histologic stains. Two fiber types (I, II) and 3 subtypes (IIA, IIB, IIC) were observed, using CaATPase-, nicotinamide-adenine dinucleotide-tetrazolium reductase-, periodic acid-Schiff hematoxylin-, and nonspecific esterase-stained frozen serial muscle sections. Type I muscle fibers in general had low CaATPase activity, high oxidative capacity, low glycogen capacity, and low esterase activity. Type IIA muscle fibers had high CaATPase activity, intermediate oxidative capacity, high glycogen concentration, and high esterase activity. Type IIB fibers had high CaATPase activity, low oxidative capacity, high glycogen concentration, and a high esterase activity. Type IIC muscle fibers had high CaATPase activity, high oxidative capacity, variable glycogen concentration, and high esterase activity. Type II (IIA and IIB) muscle fibers predominated in the muscles. The percentage of muscle fiber population, mean minimal muscle fiber diameter, and percentage of relative muscle fiber area were determined for each sampled muscle. Type IIA and IIB muscle fibers predominated in the percentage of muscle fiber population and percentage of relative muscle fiber area. Type IIB muscle fibers had the greatest minimal fiber diameter, type IIA muscle fibers had intermediate minimal fiber diameter, and type I muscle fibers had the smallest minimal fiber diameter. The percentage of relative muscle fiber area was less variable (P less than or equal to 0.05) than the percentage of muscle fiber population. Mean muscle fiber diameter did not significantly differ between breeds. Alkaline and acid phosphatase activities were at low levels in all muscles biopsied and were limited to the IM connective tissue fibrocytes, macrophages, and capillaries.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Histochemical staining characteristics of normal horse skeletal muscle. 375 94

Temporal and spatial patterns of lipid deposition, vascularization and collagen deposition were described for subcutaneous adipose tissue in the fetal pig. Enzyme cytochemical changes were reported as they relate to the morphological differentiation of the subcutaneous depot. There are distinct temporal lags between the appearance of specific enzymes in adipocytes. For example, NADH-tetrazolium reductase activity appeared earliest whereas esterase activity appeared before lipoprotein lipase (LPL) activity. Adipose tissue primordia has been localized around specific tissue components in rat and pig tissues. These tissue components include hair follicles, sweat glands, large nerves, large blood vessels and mammary gland ducts. Lipid and enzyme cytochemistry demonstrates physical continuity between primordial cells and differentiated fat cell clusters. Alterations in maternal and/or fetal endocrine or metabolic profiles result in specific changes in fetal subcutaneous adipocytes. For example, maternal diabetes significantly increases cell size whereas genetic obesity has little effect on cell size but increases cellular LPL activity significantly. A comparison of subcutaneous and perirenal depots in the pig fetus indicated several depot specific anatomical and enzyme histochemical traits. Blood vessel architecture and vascular alkaline phosphatase activity clearly demarcated perirenal and subcutaneous depots in the fetus. These data indicate that site to site variations of adipose tissue characteristics may be reflecting intrinsic stromal-vascular aspects of specific locations.
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PMID:Anatomical and enzyme histochemical differentiation of adipose tissue. 393 90

3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, the enzyme catalyzing the rate-limiting step in cholesterol biosynthesis, exists in one active (dephosphorylated) and one inactive (phosphorylated) form in liver microsomes obtained from several animal species. The present study was undertaken in order to determine a) whether the human enzyme also exists in active and inactive readily interconvertible forms; b) whether the large inter-individual variation in HMG-CoA reductase activity observed in normal man can be explained by variations in the activation state of the enzyme; and c) to characterize the reactivity of antibodies raised against rat liver HMG-CoA reductase with the intact human microsomal enzyme. HMG-CoA reductase activity, assayed in microsomes prepared in the presence of 50 mM NaF, was only 17 +/- 3% of the activity observed in microsomes prepared from the same liver in the absence of fluoride. Preincubation of microsomes prepared in NaF with alkaline phosphatase resulted in a tenfold increase of enzyme activity, while the activity of microsomes prepared without fluoride was increased also (by about 45%) with this treatment. On the other hand, the activated enzyme could be inactivated by incubation of microsomes with Mg-ATP. In eleven normal weight, normolipidemic gallstone patients, the HMG-CoA reductase activity determined in microsomes prepared without NaF ("standard procedure") reflected well both the "expressed" activity (in microsomes prepared with NaF) and the "total" (fully activated) enzyme activity; correlation coefficients were +0.80 and +0.84, respectively. Preincubation of human liver microsomes with rabbit antiserum against partially purified HMG-CoA reductase from rat liver resulted in a 72 +/- 6% inhibition of enzyme activity.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:3-hydroxy-3-methylglutaryl coenzyme A reductase in human liver microsomes: active and inactive forms and cross-reactivity with antibody against rat liver enzyme. 608 40


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