Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Crude extracts of triple-cloned, purified cultures of 22 species of Mycoplasma and Acholeplasma were examined for expression of 21 isozyme systems routinely used to type mammalian cells. Nine previously described enzymes (purine nucleoside phosphorylase, adenylate kinase, dipeptidase, esterase, glyceraldehyde-3-phosphate dehydrogenase, glucose phosphate isomerase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and superoxide dismutase) and three enzymes not previously reported in mycoplasma (triose phosphate isomerase, inorganic pyrophosphatase, and acid phosphatase) were detected in some or all of the species examined. These findings provide new information on the enzymatic expressions of these organisms. Three of the isozyme systems (superoxide dismutase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase) were present in Acholeplasma species but not in any Mycoplasma species. The characteristic pattern of electrophoretic mobility of the 12 isozyme systems also provides a useful biochemical property for identification, characterization, and classification of these mycoplasmas. Mycoplasma isozyme expression for seven of the enzymes were readily detected in various infected-cell culture lines by using either cell extracts or concentrated cell culture fluids. Mycoplasma-specific enzymes found in infected-cell extracts had the same electrophoretic mobility patterns as enzymes obtained from broth-grown mycoplasmas of the same species. Expression of homologous mammalian enzymes was not detectably altered by infection with mycoplasmas.
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PMID:Analysis of multiple isoenzyme expression among twenty-two species of Mycoplasma and Acholeplasma. 721 1

Enzyme activities of the energy supplying metabolism were investigated in muscle specimens of brachial biceps, deltoid or anterior tibial muscles of patients with traumatic nerve lesions, polyneuropathies, Charcot-Marie-Tooth disease, amyotrophic lateral sclerosis, spinal muscular atrophy and hemiparesis. The key enzymes of glycogenolysis (glycogen phosphorylase), glycolysis (triosephosphate dehydrogenase, lactate dehydrogenase), alpha-glycerophosphate cycle (alpha-glycerophosphate dehydrogenase), beta-oxidation of fatty acids (beta-hydroxy-acyl-CoA-dehydrogenase), citrate acid cycle (citrate synthase, malate dehydrogenase), hexokinase reaction (hexokinase) and pentosephosphate shunt (6-phosphogluconate dehydrogenase) were measured. The present study shows that in case of disorders of the lower motor neuron--especially those with impaired axoplasmic transport--changes in the enzyme patterns of muscles occur at an early stage. The glycolytic enzyme activities are of particular significance because they are the most sensitive indicators of the onset, extent and course of neurogenic atrophy. There is a good correlation between severity of the lesion, functional state of the muscles and reduction of these enzyme activities. In case of traumatic nerve lesions re-innervation can prevent a permanent reduction of glycolytic enzymes only if it occurs during the first months after denervation. In all cases in which operative revision is considered, it is therefore not advisible to wait since the regenerative capacity of the motor neuron is not the only limiting factor but also the biochemical and morphological changes in the muscle fibre. These are permanent after long lasting denervation without re-innervation within the first months. Primary neuroaxonal degeneration of the nerve fibre which was found in the majority of our alcoholic patients obviously impairs the metabolism of the muscle to a greater extent than primary demyelination most frequently observed in diabetics with polyneuropathy. Corresponding to the chronic course of the illness over years and to the severity of the pareses, drastic reduction in the activities of glycolytic enzymes was found in patients with Charcot-Marie-Tooth disease. Simultaneously the activity of 6-phosphogluconate dehydrogenase was significantly increased as a result of the chronic neurogenic lesion of the muscle fibres. Follow-up during the treatment of diseases of the lower motor neuron can be performed because the enzyme activities can be measured even in small muscle specimens. In patients with hemiparesis slight but not significant reduction in the glycolytic enzyme activities was found by comparison with a normal control group. We assume that this reduction is due to general inactivity which is caused by the movement disorder rather than to the particular influence of the upper motor neuron.
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PMID:[Biochemical studies on muscles in neurogenic atrophies and central paralysis. Studies of the trophic functions of neurons]. 742 10

A method for the fractionation of swine erythrocytes according to age using Percoll is described. Centrifugation of erythrocytes on discontinuous Percoll gradients yielded four fractions of erythrocytes. To ascertain that each fraction of erythrocytes represented a different age group, the activities of hexokinase (Hx), aldolase, glyceraldehyde-3-phosphate dehydrogenase (GAPD), pyruvate kinase (PK), lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) were determined. These enzyme activities decreased successively from the top to the bottom fractions of the centrifuged column. Young erythrocytes obtained from the upper fractions of the centrifuged column exhibited a higher activity of each enzyme than that found in the heavier and older erythrocytes at the bottom fraction. This method is proposed as the most appropriate for use as an aid in distinguishing the presence of a young erythrocyte population.
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PMID:Swine erythrocyte fractionation in Percoll density gradients. 813 69

Effects of prolactin(Prl), bromocriptine(Br), testosterone propionate (TP), dihydrotestosterone (DHT) and combinations of these androgens with Prl/Br on the maximum catalytic capacities of seminal vesicular enzymes involved in the glycolytic and pentose phosphate pathways in castrated mature monkeys were studied. Castration decreased the activities of all of the enzymes studied such as hexokinase(HK), 6-phosphofructokinase(PFK), glyceraldehyde-3-phosphate dehydrogenase(G3PD), pyruvate kinase(PK), glucose 6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase(6PGD) in the seminal vesicles. Prl restored the activities of all of the enzymes to their normal values except G3PD. TP/DHT maintained all the enzyme activities at the normal tissue intact level. Prl given along with androgens further enhanced the androgen action with regard to all the enzymes activities except G3PD. Br decreased all of the enzymes but Br with androgens maintained all the enzyme activities at the normal level. Castration decreased significantly serum T/DHT titres but Prl did not alter Prl levels. Prl+TP/DHT elevated Prl levels. Br alone decreased serum Prl, T and DHT titres, but Br+TP/DHT decreased only Prl, elevated T and maintained DHT levels. These results suggest that Prl has a direct as well as a synergistic action with androgens on the activities of the enzymes of glycolysis and pentose phosphate pathways in the seminal vesicles of castrated monkeys.
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PMID:Effects of prolactin and androgens on enzymes of carbohydrate metabolism in seminal vesicles of castrated mature bonnet monkeys, Macaca radiata. 827 11

Among progeny of a hybrid (Rana shqiperica x R. lessonae) x R. lessonae, 14 of 22 loci form four linkage groups (LGs): (1) mitochondrial aspartate aminotransferase, carbonate dehydratase-2, esterase 4, peptidase D; (2) mannosephosphate isomerase, lactate dehydrogenase-B, sex, hexokinase-1, peptidase B; (3) albumin, fructose-biphosphatase-1, guanine deaminase; (4) mitochondrial superoxide dismutase, cytosolic malic enzyme, xanthine oxidase. Fructose-biphosphate aldolase-2 and cytosolic aspartate aminotransferase possibly form a fifth LG. Mitochondrial aconitate hydratase, alpha-glucosidase, glyceraldehyde-3-phosphate dehydrogenase, phosphogluconate dehydrogenase, and phosphoglucomutase-2 are unlinked to other loci. All testable linkages (among eight loci of LGs 1, 2, 3, and 4) are shared with eastern palearctic water frogs. Including published data, 44 protein loci can be assigned to 10 of the 13 chromosomes in Holarctic Rana. Of testable pairs among 18 protein loci, agreement between Palearctic and Nearctic Rana is complete (125 unlinked, 14 linked pairs among 14 loci of five syntenies), and Holarctic Rana and Xenopus laevis are highly concordant (125 shared nonlinkages, 13 shared linkages, three differences). Several Rana syntenies occur in mammals and fish. Many syntenies apparently have persisted for 60-140 x 10(6) years (frogs), some even for 350-400 x 10(6) years (mammals and teleosts).
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PMID:Linkage groups of protein-coding genes in western palearctic water frogs reveal extensive evolutionary conservation. 928 85

Red cells glycolytic enzymes attached and nonattached to K88+ Escherichia coli were assayed. Hexokinase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, pyruvate kinase, glyceraldehyde-3-phosphate dehydrogenase and glutathione reductase activities, were measured. E. coli with K88ab fimbriae, E. coli with K88ac fimbriae, and isolated K88ab fimbriae were investigated for their effect on the above enzymes. Different changes were obtained with K88ab + bacteria compared with K88ac + bacteria. Purified fimbriae gave a third set of responses.
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PMID:Metabolic changes in red cells in response to adhesion of porcine K88 fimbriated Escherichia coli. 945 60

(1) The effects of the neurotoxin 3-acetylpyridine on the levels of soluble proteins and enzyme activities in various tissues of Japanese quail were investigated. (2) SDS-polyacrylamide gel electrophoresis showed that in the brain the soluble proteins with a molecular mass corresponding to 18 kDa were increased in quail treated with this toxin. The soluble liver proteins with the largest molecular masses (200, 120, 98, 80.5 and 58 kDa) were either missing or present at lower concentrations in the treated group compared to those in the controls while those of lower molecular mass (62, 55, 45, 36.5 and 24 kDa) were found to be present in higher concentrations. Similarly, treatment with 3-acetylpyridine tended to decrease the concentration of soluble proteins in pectoral muscle having a high molecular mass (160, 98, 60, 33, 30.5, 22 and 14 kDa) and to increase those having a low molecular mass (26, 20, 19.5 and 16 kDa). (3) There was a marked reduction in the treatment group in the concentration of NAD in pectoral muscle but not in other tissues. A similar observation was also made with total RNAs levels. (4) The specific activity of malic enzyme and glyceraldehyde-3-phosphate dehydrogenase was markedly reduced in the liver and pectoral muscle of the treatment group but was not affected in other tissues. The specific activity of 6-phosphogluconate dehydrogenase was significantly lower in the liver only, and that of lactic dehydrogenase and acetylcholinesterase was not affected in any of the tissues examined. (5) The results suggest that the metabolic actions of 3-acetylpyridine are quite distinct from those shown by niacin deficiency and its analog such as 6-aminonicotinamide.
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PMID:Effects of the neurotoxin 3-acetylpyridine on levels of soluble proteins and enzyme activities in various tissues of Japanese quail. 967 82

The effects of niacin deficiency on the levels of soluble proteins and enzyme activities of Japanese quail have been investigated. SDS-polyacrylamide gel electrophoresis revealed that in the pectoral muscle the soluble proteins with molecular masses corresponding to 181, 128, 93, 76, 72, 62, 56, 43, 41, 28 and 20 kDa were present in lower amounts but those of 60, 50 and 37 kDa were present in higher amounts. In the heart the soluble proteins with a molecular mass of 181 kDa were present in lower amounts and in the brain those of 43 kDa were present in lower amounts but those of 221 kDa were present in higher amounts. In the intestine the soluble proteins with molecular masses corresponding to 181, 102, 83, 74, 72, 44 and 40 kDa were present in lower amounts but those of 41 kDa and 18 kDa were present in higher amounts. There was a marked reduction in the level of NAD and NADPH in the pectoral muscle of niacin deficient quail but not in other tissues. The specific activity of glyceraldehyde-3-phosphate dehydrogenase decreased markedly both in the liver and pectoral muscle of niacin deficient quail whereas that of 6-phosphogluconate dehydrogenase and malic enzyme decreased markedly in the liver or pectoral muscle, respectively. In contrast, the specific activity of acetylcholinesterase and carboxypeptidase increased markedly in the liver or the pectoral muscle, respectively. The results suggest that a severe niacin deficiency exerted specific effects on levels of some soluble proteins particularly in the pectoral muscle and intestine and on activities of certain enzymes in the liver and the pectoral muscle.
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PMID:Effects of niacin deficiency on the levels of soluble proteins and enzyme activities in various tissues of Japanese quail. 974 85

(1) The effects of long term treatment with 3-acetylpyridine on the stability of enzymes towards heat and trypsin treatment were studied. (2) In the liver NAD or NADP provided a similar degree of protection against heat inactivation at 55 degrees C for 6-phosphogluconate dehydrogenase (24%), glyceraldehyde-3-phosphate dehydrogenase (24%) and malic enzyme (20%), low level of protection of lactate dehydrogenase (13%) but didn't affect acetylcholinesterase at all. In the muscle, however, there was substantial protection against heat inactivation by coenzyme of glyceraldehyde-3-phosphate dehydrogenase (52%), an intermediate level of protection of lactate dehydrogenase (25%), low level of protection of 6-phosphogluconate dehydrogenase (17%) and malic enzyme (17%) and almost no protection of acetylcholinesterase. (3) In the susceptibility towards trypsin a low but similar degree of protection for dehydrogenases by coenzymes was observed in the liver whereas in the muscle there was substantial protection against trypsin inactivation by NAD of glyceraldehyde-3-phosphate dehydrogenase, an intermediate level of protection of 6-phosphogluconate dehydrogenase and malic enzyme and very little protection of lactate dehydrogenase but no protection of acetylcholinesterase. Among enzymes tested, glyceraldehyde-3-phosphate dehydrogenase showed the greatest protection against heat and trypsin inactivation by NAD. (4) The results suggest that the effect of 3-acetylpyridine treatment on the stability of muscle glyceraldehyde-3-phosphate dehydrogenase appears to be quite specific and selective.
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PMID:Effects of NAD or NADP on the stability of liver and pectoral muscle enzymes in 3-acetylpyridine treated quail by heat and trypsin. 983 47

The stability of liver and muscle enzymes and proteins in niacin-deficient quail towards trypsin treatment in the presence and absence of coenzymes, NAD or NADP, was characterized. The protection of liver dehydrogenases by coenzymes was low when they are subjected to trypsin digestion for 60 min. In contrast, in the muscle there was substantial protection against trypsin inactivation of glyceraldehyde-3-phosphate dehydrogenase by NAD and of 6-phosphogluconate dehydrogenase by NADP. Among all enzymes tested, glyceraldehyde-3-phosphate dehydrogenase showed the greatest protection against trypsin inactivation by NAD. SDS-polyacrylamide gel electrophoresis demonstrated that muscle proteins from the niacin-deficient group were more substantially protected compared to control and pair-fed groups when liver and muscle extracts were spiked with NAD and subjected to trypsin digestion. Overall results suggest that niacin deficiency exerted specific destabilizing effects on the stability of enzymes and proteins in muscle.
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PMID:Effects of nicotinamide coenzymes on the stability of enzyme activities and proteins in niacin-deficient quail tissues against trypsin treatment. 1116 9


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