Sample records for fructosediphosphates
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Dieter, M.P.
1974-01-01
Male Coturnix quail (Coturnix coturnix japonica) were fed diets for 12 weeks containing graded levels of DDE, polychlorinated biphenyl (Aroclor 1254), malathion, and mercuric chloride. Birds were bled prior to exposure and at 2, 4 and 12 weeks, and the plasma used to measure the activities of creatine kinase, aspartate aminotransferase, cholinesterase, fructose-diphosphate aldolase, and lactate dehydrogenase. Abnormal activity of certain plasma enzymes was noted in birds after 2 and 4 weeks, but these changes were not proportional to dose or exposure time. At 12 weeks increases in each of the activities of plasma enzymes of birds fed organochlorines, and decreases in cholinesterase activity of birds fed malathion or mercuric chloride, were proportional to the log dose of the respective agents. In addition, the pattern of enzyme responses in the 4 experimental groups had changed, and was illustrative of the specific type of substance that had been fed. The data suggest that qualitative and quantitative identification of environmental contaminants in birds, and perhaps a variety of wild animals, may be possible by utilization of multiple plasma enzyme assays. Residue analyses after 12 weeks of feeding showed that DDE accumulated in carcasses and livers at concentrations up to 4-fold higher than those in the diets. In contrast residues of Aroclor 1254 attained in carcasses were identical to, and in livers one-half of, the concentration in the feed. Mercury did not accumulate as much in the tissues; residues attained were one-twentieth or less of those in the feed.
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Yu, Panxi; Diao, Wenqi; Tang, Qionglan; Jiang, Xuefeng
2015-09-14
Pregnancies in hemodialysis patients are uncommon and difficult to study. Although the chance of a successful pregnancy and parturition in hemodialysis women has increased over the years, it still remains extremely low with a high maternal and fetal mortality and morbidity rate. We reported a case of successful pregnancy and parturition in a 22-year-old Chinese female in uremic stage of chronic renal failure and undergoing maintenance hemodialysis (three sessions a week) for 6 years. At the 22nd gestational week, she was diagnosed as pregnant by ultrasound, and started an enhanced hemodialysis routine (Five sessions a week). At the 32nd gestational week, she got hospitalized and received hemodialysis more frequently (seven sessions a week). Based on the initial diagnoses, including uremic stage of chronic renal failure, stage-3 hypertension, single pregnancy of 32nd gestational week, single umbilical artery and polyhydramnios, a drug therapy consisting of compound amino acid, fructosediphosphate sodium, 10% L-carnitine, erythropoietin, polyferose, amlodipine, isosorbidedinitrate, low-molecular weight-heparin, multivitamins and folic acid was given, and daily examination of the mother and fetus was performed. Under the joint efforts of various departments, the patient underwent caesarean section at the 34th gestational week due to progressive uterine contraction and gave birth to a female, well-being baby weighing 1470 g. It has been more than 3 years since the parturition. The mother has returned to the previous hemodialysis routine, and the child has been growing up healthily. Although pregnancy in hemodialysis patients is rare, with a high rate of risks. Patients could still gain a good outcome, if we intensify hemodialysis and enhance the collaboration between the patient, nephrologists, obstetricians, neonatologist, nutritionists, and other departments.
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The reduction of retinene1 to vitamina A1 in vitro.
WALD, G; HUBBARD, R
1949-01-01
In the surviving vertebrate retina the retinene(1) liberated by bleaching rhodopsin is converted quantitatively to vitamin A(1). Recent chemical studies have indicated that in this process the aldehyde group of retinene(1) is reduced to the primary alcohol group of vitamin A(1) (Morton; Wald). Some time ago we brought this reaction into a cell-free brei prepared from cattle retinas. The retinas were frozen, desiccated, ground, and exhaustively extracted with petroleum ether; the resulting powder, stirred in neutral buffer solution and exposed to light, converted its retinene(1) completely to vitamin A(1). Some time ago also we observed that fresh rhodopsin solutions exhibit a special type of fading in darkness following exposure to light, which is absent from the same solutions after aging. We have confirmed Bliss's identification of this reaction as the conversion of retinene(1) to vitamin A(1). The system which reduces retinene(1) is fractionated anatomically in the retinal rods. The outer segments of the rods, broken off from the underlying retinal tissue, are unable to convert their retinene(1) to vitamin A(1). In the presence of a water extract of crushed retina they do perform this conversion. On the other hand the retinal tissue from which a water extract was taken has lost this capacity. Such washed retinal tissue is reactivated by returning the washings to the solid material. The activating effect of retinal washings on isolated outer limbs or washed retina is duplicated by a boiled muscle juice. This in turn can be replaced by reduced cozymase (reduced coenzyme I; DPN-H(2)); or by a mixture of DPN and fructosediphosphate. The conversion of retinene(1) to vitamin A(1) is therefore a reduction in which two atoms of hydrogen are transferred to retinene(1) from reduced cozymase. It is assumed that this reaction is catalyzed by an apoenzyme, retinene(1) reductase, present in the rod outer limb. This process is coupled with a second system in the outer segment which reduces DPN, using hexosediphosphate or one of its derivatives as hydrogen donor. This action of DPN brings a member of the vitamin B complex, nicotinic acid amide, into an auxiliary position in the rhodopsin system. In the isolated retina or in vitro systems the reduction of retinene(1) proceeds irreversibly. Yet this reduction must be balanced by an oxidative process elsewhere in the rhodopsin cycle, since through rhodopsin as intermediate vitamin A(1) regenerates retinene(1).