Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The production of neuraminidase by a classical strain of Clostridium welchii (C. perfringens) type A was studied. Good yields were produced in 5% Proteose Peptone-water medium (PPW5); the enzyme was essentially extracellular but some further neuraminidase could be released by ultrasonic disintegration of the cells. This also released N-acyl neuraminic acid-aldolase (NAN-aldolase) and the degree to which this interferes with the assay for neuraminidase was evaluated. Forty-one British reference food-poisoning strains of C. welchii type A were examined for extracellular neuraminidase production in PPW5. Twelve of 17 strains that produce so-called heat-sensitive spores were neuraminidase positive whereas 20 of 24 strains that are non-haemolytic and produce very heat-resistant sporeswere neuraminidase negative. Variation was found in the ability to produce neuraminidase among strains of a single Hobbs' serotype; four Hobbs' type-13 strains produced neuraminidase but a fifth did not. Disruption of the cells of a Hobbs' type-2 strain that did not produce any extracellular neuraminidase released NAN-aldolase but there was no evidence of cell-associated neuraminidase. British food-poisoning strains of C. welchii type A thus include some that are clearly neuraminidase positive and some that still cannot be shown to produce neuraminidase. There is no correlation between lack of neuraminidase production and the ability to cause food poisoning, although the majority of non-haemolytic heat-resistant strains do not produce neuraminidase. It remains possible that neuraminidase may play a part in C. welchii gas gangrene; it is suggested that the ability to define neuraminidase-negative strains may now be of value in investigating this possibility.
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PMID:The production of neuraminidase by food poisoning strains of Clostridium welchii (C. perfringens). 16 69

The stereochemical course of the formation of the alkyl ether bond in alkyl ether lipids was investigated through the synthesis of stereospecifically labeled acyl R- or S-[1-3H]dihydroxyacetone 3-phosphate (DHAP) starting from L-glyceraldehyde. It was demonstrated directly that the formation of the alkyl ether bond results in the stereospecific exchange of the pro-R C-1 hydrogen of DHAP with a proton of water. The configuration of the hydrogen that is retained on C-1 after formation of the alkyl ether bond was also investigated. The alkyl ether lipid was degraded, and the DHAP backbone isolated as glycerol, converted to DHAP via glycerol 3-phosphate and treated with either aldolase or triose phosphate isomerase. The results demonstrated that the retained hydrogen on C-1, which was pro-S in the starting substrate, was pro-S in the product alkyl ether.
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PMID:Stereochemical specificity of the biosynthesis of the alkyl ether bond in alkyl ether lipids. 43 13

A partially purified preparation of a water-soluble, heat-resistant, nonspecific exotoxin produced by a strain of Macrophomina phaseolina, isolated from Phaseolus mungo L. could reduce Cu++ ions and produced a red colour with 2,4-dinitrophenyl hydrazine reagent. It caused inhibition of seed germination, wilting of cult seedlings, stunted growth of young seedlings and loss of permeability of the cell membrane. Seedlings of P. mungo, grown in presence of the toxin showed a slight increase in the contents of protein and total RNA over control, but a significant increase in the specific activities of F-1, 6-BP aldolase and G-6-P isomerase.
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PMID:Purification and properties of heat-resistant exotoxin produced by Macrophomina phaseolina (Tassi) Goid in culture. 48 87

To determine the effect of chronic alcohol ingestion, rats were given 15 or 25% v/v of alcohol in water for a period of 6 months. The activities of some key enzymes involved in the metabolism of glucose, mitochondrial respiratory rates, and efficiency of oxidative phosphorylation were studied in the hearts of alcohol-treated and untreated rats. In the group receiving 15% alcohol, glucose-6-phosphate dehydrogenase (G-6-PDH) was elevated. In rats given 25% alcohol, activities of G-6-PDH, aldolase, and glyceraldehyde phosphate dehydrogenase were elevated but isocitrate dehydrogenase was reduced. Mitochondrial respiratory rates and the efficiency of phosphorylation were depressed in rats given 25% of alcohol. Except for mitochondrial oxidation of pyruvate and alpha-ketoglutarate, all biochemical parameters studied were within normal limits a month after alcohol was discontinued.
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PMID:The effect of chronic ethanol ingestion on myocardial glucose and energy metabolism. 56 91

Although a neuromuscular syndrome has been induced experimentally by vitamin E deficiency, a human syndrome has not yet been documented. This report describes a 7-year-old boy with severe malabsorption since birth who presented with progressive external ophthalmoplegia, proximal muscle weakness, peripheral neuropathy, hyporeflexia, and bilateral Babinski signs. Abnormalities on neurologic examination included elevated creatine phosphokinase and aldolase, slowed distal sensory latencies, type II muscle fiber atrophy, and a plasma vitamin E level of 8 microgram per deciliter (normal, 550-1500 microgram per deciliter). Treatment with oral water-solubilized vitamin E (400 IU daily; greater than 50 times the normal daily intake) was begun, with repeat laboratory studies at 3-month intervals. Over a 16-month period, plasma vitamin E content gradually increased to 350 microgram per deciliter, associated with declining sarcoplasmic enzyme activities and clinical improvement.
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PMID:Reversibility of human myopathy caused by vitamin E deficiency. 57 10

Adenylate cyclase from purified beef thyroid membranes has been solubilized by the use of Triton N-101 after preactivation with guanosine 5'-(beta, gamma-imido)-triphosphate. The soluble activity passed a 0.22- micron filter, was not sedimented at 100,000 X g for 2 h, and behaved like aldolase in sucrose density gradients and on Sepharose 6B. From comparison of the sedimentation in D2O and H2O the partial specific volume was found to be like that of globular proteins (0.75 +/- 0.006), hence little detergent appeared to be bound to the enzyme. The sedimentation coefficient was 7.4 +/- 0.15, the Stokes radius 45 A, and the molecular weight 159,000. Prestimulation by thyrotropin did not survive solubilization. The stimulation produced by guanosine 5'-(beta, gamma-imido)triphosphate persisted as did the more active state resulting from pretreatment with both this nucleotide plus thyrotropin. Thyrotropin did not stimulate the solubilized enzyme. The Km for ATP, thermal stability, and inhibition by Ca2+ were identical for the membrane-bound and soluble enzyme, while the pH optimum was increased 0.5 unit in the latter. Polyanions and phenothiazines inhibited both preparations equally, whereas only membranes responded to stimulation by polylysine and ribonuclease.
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PMID:Soluble adenylate cyclase from thyroid membranes. 67 Jan 96

The partial specific volume, upsilon20, of bovine serum albumin at 25 degrees C was found to be 0.728 +/- 0.001 ml/g in solutions of guanidine hydrochloride (GuHC1), 0.01 M dithioerythritol (DTE), independent of GuHC1 concentration (3-6 M). The volume decrease upon denaturation is about 400 ml/mol (upsilon20 in water at the same temperature was found to be 0.734). From the reduced density increments at constant chemical potential of diffusible solutes, The apparent volumes, phi, were found to increase from 0.693 ml/g at 3 M GuHC1 to about 0.725 ml/g at 7 M GuHC1. The phenomenological interaction parameter, xi3 (grams of GuHC1 "bound" per gram of protein), was found to decrease from about 0.2 at 3 M GuHC1 to about 0.07 at 6.4 M GuHC1. The phenomenological interaction parameter, xi1 (grams of water "bound" per gram of protein), is negative and become less negative with increase in GuHC1 concentration. The relation between xi3 and xi1 and physical binding and exclusion of low-molecular-weight components are discussed in terms of simple model consideration. It is concluded that over the range of GuHC1 concentrations studied about 0.2 g of water as well as 0.28 g of GuHC1 are bound per gram of protein. This corresponds on the average to 1.3 molecules of water and 0.35 molecule of GuHC1 per amino acid residue. Similar results were found by recalculating some previous results for aldolase. These results on proteins in GuHC1 solution are in marked contrast to the behavior of DNA at high concentrations of NaCl and CsCl, which is analyzed on the basis of earlier work.
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PMID:Bovine serum albumin and aqueous guanidine hydrochloride solutions. Preferential and absolute interactions and comparison with other systems. 83 84

Setaria cervi, the filarial parasite inhabiting the Indian water buffalo (Bubalus bubalis Linn.) contained almost all the enzymes involved in glycogen degradation. Significant activities of glycogen phosphorylase, glucokinase, phosphoglucomutase, phosphoglucose isomerase, phosphofructokinase, FDP-aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate hydratase, pyruvate kinase, lactate dehydrogenase glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were detected in cell-free extracts of whole worms. The presence of PEP-carboxykinase, malate dehydrogenase, fumarase and fumarate reductase revealed the functioning of the PEP-succinate pathway in addition to phosphorylating glycolysis and pentose phosphate pathway in the parasite. Excepting fumarate reductase all other enzymes were localized in the particulate-free cytosol fraction, although small amounts of glycogen phosphorylase, aldolase and lactate dehydrogenase were also detected in the mitochondrial fraction.
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PMID:Setaria cervi: enzymes of glycolysis and PEP-succinate pathway. 86 May 72

Rabbit muscle aldolase catalyzes the exchange with solvent of all three methyl hydrogens of hydroxyacetone phosphate. Under saturating conditions, rates of the following processes have been measured: deuteration of hydroxyacetone phosphate in 2H2O (by an NMR method), tritiation of hydroxyacetone phosphate in H2O and 2H2O, and detritiation of tritiated hydroxyacetone phosphate in H2O and 2H2O. It is clear from these measurements (1) that there is no primary kinetic isotope effect and hence that hydrogen abstraction is not rate determining to the exchange and (2) that only one (as the closest integer) methyl hydrogen exchanges per turnover. The argument is made that these observations are mutually exclusive in terms of the accepted aldolase mechanism in the absence of further restrictions imposed by the enzyme. Possible restrictions are discussed.
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PMID:Rabbit muscle aldolase catalyzed proton exchange of hydroxyacetone phosphate with solvent. 91 52

A study was made of changes in outflux, extractability and enzyme (aldolase and creatine kinase) activity of muscle proteins induced by thermal action in skeletal muscles of R. temporaria L. Under a 15-minutes action of temperatures under 36 degrees C, which do not produce any contracture or fall of excitability, changes in a fraction of protein outfluxed from muscles were observed. The thermal action accompanied by the fall and irreversible loss of excitability (above 36 degrees) resulted in the fall of extractability and enzyme activity of water-soluble proteins extracted from homogenized muscles in addition to prolonged changes in the fraction of outfluxed proteins. The increased binding of aldolase by actomyosin under thermal injury of muscle is established. Changes of outflux extractability and enzyme activity of proteins during the thermal alteration of muscle are considered with regard to data about the complexing of muscle proteins.
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PMID:[Changes in aldolase and creatine kinase activity during thermal muscle damage]. 92 97


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