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:4.1.2.13 (aldolase)
3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A study was made of solubilization of aldolase isolated from homogenates of skeletal muscles, both intact and being in the state of contracture due to urea action. Compared to water, electrolytes extract more aldolase from homogenates of intact and altered muscles. Almost the same amounts of aldolase were extracted with electrolytes from homogenates of muscles, which lost irreversibly their excitability, and of intact muscles. The actomyosin isolated from muscles displayed aldolase activity not removed under reprecipitation. The aldolase activity of actomyosin, the increase in sorption activity of proteins due to their conformational changes, and the decrease in excitability of aldolase isolated from homogenates of altered muscles by urea doses inducing denaturation of actomyosin and aldolase, all this may suggest that the action of injured agents on muscle stimulates the ability of aldolase and actomyosin to interact. The ratio of free and bound forms of aldolase differs in the intact and in the altered muscle cell.
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PMID:[Nature of the changes in water-soluble enzyme activity in the action of injurious agents on the muscles. II. The change in the extractability of aldolase from muscles exposed to urea]. 660 56

Band 3 is the predominant membrane-spanning polypeptide and the mediator of anion transport in the human erythrocyte. In addition, it provides the sites of association for fructose 1,6-bisphosphate aldolase and other cytoplasmic proteins with the membrane. The aldolase-binding activity of water-soluble fragments of band 3 was measured by their inhibition of aldolase catalytic activity and by their displacement of aldolase from ghosts. At saturation, the binding of one band 3 or certain of its fragments per aldolase molecule partially inhibited the catalytic activity and band 3 binding of the unliganded subunits of the tetramer through an apparently cooperative mechanism. An NH2-terminal 23,000-dalton fragment generated by S-cyanylation of the cytoplasmic pole of band 3 was approximately 20% as avid in binding aldolase as was native band 3. Several fragments cleaved from the NH2-terminal portion of the 23,000-dalton peptide by trypsin, mild acid hydrolysis, and cyanogen bromide digestion all bound aldolase, while fragments from the rest of the polypeptide were essentially inactive. The first 31 residues of band 3 contained 16 Asp plus Glu, no basic residues, and a blocked alpha-amino terminus. The highly acidic composition of this region is consistent with the strongly electrostatic character of the interaction between band 3 and aldolase, presumably at the strongly basic catalytic center of the enzyme. We conclude that the NH2-terminal region of band 3 bears the membrane-binding site for aldolase.
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PMID:The aldolase-binding site of the human erythrocyte membrane is at the NH2 terminus of band 3. 728 63

The multicomponent solution, containing 15% of glycerol, 4.5% of proteins, 0.9% of sodium chloride, 0.33% of potassium chloride and water for injections, was proposed. The ferments activity (aminotransferases, cholinesterase, aldolase, alkaline phosphatase), blood coagulating system state (the prothrombin level, plasma tolerance, her recalcification time), the mineral elements contents (potassium, sodium, calcium), the contents of protein and its fractions in blood before and after an acute blood loss compensation with the multicomponent solution, and also its influence on the animals organism in prolonged daily (during 30 days) intravenous injection were studied. The combination of components in the solution permit to store the studying indexes on level close to initial; if the loss of blood compensates in the first hours, high survival of animals is insured. Negative reactions of organism while prolonged intravenous injection of the multicomponent solution are not revealed.
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PMID:[Use of glycerin as a component of the solution in treating acute hemorrhage]. 760 2

For a given biochemical transformation, such as the fermentation reaction, the redistribution coefficients, which relate the natural site-specific isotope contents in end products to those of their precursors, are a source of mechanistic information. These coefficients characterize the traceability of specific hydrogens in the products (ethanol and water) to their parent hydrogens in the starting materials (glucose and water). In conditions of complete transformation, they also enable intermolecular exchanges with the water medium to be estimated. Thus it is directly confirmed that hydrogens 1, 2, 6, and 6' of glucose are strongly connected to the methyl site I of ethanol obtained by fermentation by Saccharomyces cerevisiae. However, whereas hydrogens 6 and 6' are transferred to a great extent, transfer is only partial for hydrogen 2, and it is even less for hydrogen 1. Because the two moieties of glucose corresponding to carbons 1-2-3 and 4-5-6 are scrambled by the aldolase and triosephosphate isomerase reactions, additional exchange of hydrogens at positions 1 and 2 must have occurred before these steps. The value of the coefficient that relates site 2 of glucose to site I of ethanol in particular can be used to quantify the contribution of intermolecular exchange occurring in the course of the transfer from site 2 of glucose 6-phosphate to site 1 of fructose 6-phosphate mediated by phosphoglucoisomerase. The average hydrogen isotope effects associated with the transfer of hydrogen from the water pool to the methyl or methylene site of ethanol are estimated. In contrast to conventional experiments carried out in strongly deuterium-enriched media where metabolic switching may occur, the NMR investigation of site-specific natural isotope fractionation, which operates at tracer isotopic abundance, faithfully describes the unperturbed metabolic pathways.
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PMID:Site-specific isotope fractionation in the characterization of biochemical mechanisms. The glycolytic pathway. 760 63

The effects of vanadate, an oxidized form of vanadium, on glucose metabolism of the lens in diabetic rats were studied. Five-week-old male Sprague-Dawley rats were rendered diabetic with intraperitoneal injection of streptozotocin (50 mg/kg). One week later, the diabetic rats were given 0.2 g/l NaVO3 -5g/l NaCl solution in drinking water ad libitum for 2 weeks and biochemical parameters in their lenses were determined. Blood glucose levels significantly decreased in the vanadate-administered diabetic rats (DV group), compared with the diabetic rats given no vanadate (D group). In the DV group, a significant decrease was observed in lens fructose content compared with the D group. Lens ketohexokinase activity tended to be higher and lens aldolase activity was significantly higher in the DV group than in the D group. These results indicate that vanadate accelerates the metabolic reaction from sorbitol pathway to glycolysis.
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PMID:[Effects of vanadate on glucose metabolism in the lens of rats with streptozotocin-induced diabetes--ketohexokinase and aldolase activity]. 788 27

Membrane-mediated excessive intracellular calcium accumulation (EICA) is a fundamental pathogenetic event associated with chronic muscle degeneration in patients with Duchenne muscular dystrophy (DMD), and in animals with hereditary muscular dystrophy (HMD). Because of potential Ca(2+)-channel blocking properties, we investigated the relative efficacies of chronic diltiazem (DTZM) (50 mg/kg/d), nifedipine (NFDN) (6 mg/kg/d), and verapamil (VPML) (25 mg/kg/d) therapies in reducing EICA and improving dystrophic pathobiology beginning in 30-day-old male BIO-14.6 strain dystrophic hamsters (DH). Each agent, and sterile distilled water as vehicle control, was given in a single daily oral dose for 180 days to four groups each of DH and BIO-F1B strain normal hamsters (NH). Plasma [Ca] and [Mg]; plasma aldolase (ALD), creatine kinase (CK), and lactate dehydrogenase (LDH) activities; relative cardiac hypertrophy and relative soleus hypertrophy; tissue [Ca] and [Mg] of the heart and rectus femoris muscle, histology of rectus femoris, and overall mortality rate were quantitated. Muscle Mg was not modified in DH, or by any of these agents. NFDN produced significant edema in the soleus and myocardium. During the 6-month therapeutic trial, 45% DH and 18% NH died on VPML, 27% DH and 9% NH on NFDN, and 20% DH controls on distilled water, but none on DTZM; suggesting that DTZM treated DH lived longer than DH controls. Relative efficacy in regulating EICA in both the cardiac and skeletal muscles; plasma ALD, CK, and LDH; and improving associated dystrophic pathobiology was found to be DTZM >>> NFDN > VPML. DTZM appears to be the most effective and safest agent in mitigating EICA in cardiac and skeletal muscles, efflux of intracellular enzymes, histopathology of dystrophic muscle with sporadic necrosis, and chronic muscle degeneration in DH with HMD. DTZM therapy also halted the high morbidity and mortality associated with the dystrophic pathobiology inherent in DH.
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PMID:Regulation of membrane-mediated chronic muscle degeneration in dystrophic hamsters by calcium-channel blockers: diltiazem, nifedipine and verapamil. 846 95

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

The covalent immobilization of some proteins (ovomucoid from duck egg white, human serum albumin, aldolase and thiroglobulin) on the surface of polyethylene grafted with polyacrylic acid has been studied. Water-soluble carbodiimide was (1-ethyl-3-(3-dimethylaminopropyl carbodiimide) used as a condensing agent. It was shown that three different reactions can occur in the reaction mixture during immobilization: the reaction between carboxy groups of graft copolymer and amino groups of protein (the immobilization reaction itself) and reactions between carboxy and amino groups of protein molecules (reactions of intra- and intermolecular cross-linking). The reaction of intramolecular cross-linking leads to a decrease in the physiological activity of the immobilized substance, while other reactions do not affect it. The preliminary activation of this surface by carbodiimide before the modification allows to maintain the activity after immobilization on the insoluble surfaces.
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PMID:Chemical modification of polymers with physiologically active species using water-soluble carbodiimides. 967 48

Rhabdomyolysis is a condition affecting body homeostasis that results from impaired supply of muscles with energy, nutritional factors and blood. Complex pathophysiological mechanism causes that extended myolysis may complicate different clinical conditions, such as: crush syndrome, excessive physical effort (work, seizures), toxic effect of drugs and toxins, water-electrolyte disturbances, congenital enzymatic deficiencies etc. It seems that on the cellular level, essential role is played by excessively high intracytoplasmatic calcium level, which affects metabolic processes. So high calcium level is a consequence of muscular cell injury irrespective to its reason. It manifests clinically as muscular weakness, pal and oedema and laboratory tests reveal elevated CK, GOT, GPT, aldolase and LDH levels as well as dark brown urine colour. Demonstration of elevated serum myoglobin level or its presence in urine directly confirms development of rhabdomyolysis. In unfavorable conditions, rhabdomyolysis may result in acute renal failure. Appropriately early and adequate water supply and alkalization plays an essential role in prevention of impairment in renal function. In advanced phase of renal failure, hemodialysis is a standard treatment.
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PMID:[Rhabdomyolysis: clinical features, causes, complications and treatment]. 974 Nov 96

Rabbit muscle aldolase is a homotetramer in which the subunits have a classical alpha/beta-barrel structure and Mr 39,212 Da. We have previously reported that aldolase incubated in 3 M urea has three unfolding domains distinguished by their different unfolding rates. The unfolding rates of these domains were determined from isotope patterns in the mass spectra of peptic fragments derived from aldolase incubated in 3 M urea and pulse labeled in (2)H2O. The present study extends this investigation to more thoroughly characterize the structures of these unfolding intermediates. Mass spectra of intact monomers had four envelopes of isotope peaks corresponding to four structural forms of aldolase. Analysis of the present results suggests that these structural forms consist of native aldolase and three forms that have one to three domains unfolded. The molecular masses of these four structural forms indicate that there are 107 residues in each of the three unfolding domains of aldolase. Present results also show that aldolase remains a tetramer in 4 M urea, even though hydrogen exchange and circular dichroism indicate that it has lost most of its secondary and tertiary structure. The abundances of unfolded domains, which were determined from mass spectra of either intact aldolase or its peptic fragments, were used to determine the abundances of specific, partially unfolded forms of aldolase. Kinetic modeling of the abundances of these structures suggests that these structures are formed sequentially as aldolase unfolds in urea.
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PMID:Hydrogen exchange demonstrates three domains in aldolase unfold sequentially. 1055 43


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