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)

The binding of 2-[(2-bis-[carboxymethyl]amino-5-methylphenoxy)-methyl] 6-methoxy-8-bis[carboxymethyl] aminoquinoline, the fluorescent calcium probe Quin2, to serum albumin and several other proteins has been investigated. Changes in fluorescence emission spectra and fluorescence anisotropy revealed interactions between Quin2 and several proteins including human serum albumin, bovine serum albumin, aldolase, phosphoglucose isomerase, glyceraldehyde-3-phosphate dehydrogenase, and alkaline phosphatase. Protein-probe interactions were inhibited by the presence of calcium. Binding was also measured by resonance energy transfer and gel permeation chromatography. Equilibrium binding constants for Quin2 were quantitated by the application of the recently-developed "SPECTRABIND' program to spectroscopic data (D. Toptygin and L. Brand, Anal. Biochem., 224 (1995) 330-338). Binding of Quin2 to human serum albumin is discussed in terms of the published X-ray crystal structure of human serum albumin (X.M. He and D.C. Carter, Nature, 358 (1992) 209-215).
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PMID:Steady-state and time-resolved fluorescence measurements for studying molecular interactions: interaction of a calcium-binding probe with proteins. 896 69

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

Of the 10 chronic haemodialysis patients whose serum TnT levels exceeded the threshold value of 0.1 microg.L(-1) at entry into the study, four were dead at 1 year and three others had a diagnosis of CAD. Of the 20 chronic haemodialysis patients with normal serum TnT levels at entry, one died and none had CAD. All five deaths were cardiac related, either arising from acute myocardial infarction or by sudden death. When serum TnT levels were compared with accepted predictors of death in chronic haemodialysis patients, such as serum creatinine, serum albumin and haematocrit, in the present study serum TnT proved to be more accurate and had excellent sensitivity and specificity. Serum TnT was also superior to serum TnI, which proved to be no more discriminating than the non-specific muscle marker, aldolase.
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PMID:Troponin T, a predictor of death in chronic haemodialysis patients. 985 37

Alpha-synuclein, a major constituent of Lewy bodies (LBs) in Parkinson's disease (PD), has been implicated to play a critical role in synaptic events, such as neuronal plasticity during development, learning, and degeneration under pathological conditions, although the physiological function of alpha-synuclein has not yet been established. We here present biochemical evidence that recombinant alpha-synuclein has a chaperone-like function against thermal and chemical stress in vitro. In our experiments, alpha-synuclein protected glutathione S-transferase (GST) and aldolase from heat-induced precipitation, and alpha-lactalbumin and bovine serum albumin from dithiothreitol (DTT)-induced precipitation like other molecular chaperones. Moreover, preheating of alpha-synuclein, which is believed to reorganize the molecular surface of alpha-synuclein, increased the chaperone-like activity. Interestingly, in organic solvents, which promotes the formation of secondary structure, alpha-synuclein aggregated more easily than in its native condition, which eventually might abrogate the chaperone-like function of the protein. In addition, alpha-synuclein was also rapidly and significantly precipitated by heat in the presence of Zn2+ in vitro, whereas it was not affected by the presence of Ca2+ or Mg2+. Circular dichroism spectra confirmed that alpha-synuclein underwent conformational change in the presence of Zn2+. Taken together, our data suggest that alpha-synuclein could act as a molecular chaperone, and that the conformational change of the alpha-synuclein could explain the aggregation kinetics of alpha-synuclein, which may be related to the abolishment of the chaperonic-like activity.
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PMID:Structural changes in alpha-synuclein affect its chaperone-like activity in vitro. 1120 70

A N,N-dimethylacrylamide-based hydrogel (2) with the new cross-linker (ethylenedioxy) bis[2,2'-(N-acryloylamino)ethane] (1) has been prepared, and its physicochemical properties in aqueous solution were studied. Three different native proteins (lysozyme, bovine serum albumin, and rabbit IgG) were encapsulated within the polymeric matrix 2, and the kinetics of their release from the swollen hydrogel were determined. The rate of protein release exhibits a clear dependence on both the molecular weight of the protein and the amount of cross-linker utilized to prepare the hydrogel. This is reflected by the fact that the low molecular weight proteins are released at an increased rate versus higher molecular weight proteins. In addition a greater amount of protein is released from the hydrogels with a lower percentage of cross-linker. The polymerization procedure used in this study is sufficiently mild to safeguard the functional integrity of attendant biomolecules as determined by the retention of catalytic activity of encapsulated alpha-chymotrypsin and aldolase catalytic antibody 38C2. The potential utility of these hydrogels for the controlled release of bioactive agents in vivo is strengthened by both their lack of toxicity against human dermal fibroblasts and their lack of immunogenicity in mice.
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PMID:A tunable hydrogel for encapsulation and controlled release of bioactive proteins. 1188 10

A human cDNA library was constructed using M13 derivative vectors. The simple and rapid procedures for sequencing single-stranded DNA by the dideoxy chain termination method allowed a screening of individual clones directly by DNA sequence analysis. Some of these clones were identified as coding for: serum albumin, alpha1-antitrypsin, retinol-binding protein, prothrombin, haptoglobin, and metallothionein. Furthermore, a clone coding for aldolase B was tentatively identified on the basis of high sequence homology with rabbit muscle aldolase.
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PMID:Cloning of several cDNA segments coding for human liver proteins. 1189 9

Using a test mixture consisting of standard proteins (cytochrome c, chymotrypsinogen A, hen egg albumin, bovine serum albumin, aldolase, catalase and ferritin) and synthetic polypeptides (polylysine, polyaspartic, polyglutamic acid and polyproline) it was revealed that using sodium dodecyl sulfate (SDS) as background electrolyte modifier at acid pH (2.5) allows selective separation of highly positively charged polypeptides (polylysine) provided that their relative molecular mass is sufficiently low (3300 Da). The altered elution sequence of standard proteins as compared to a separation done without SDS may help their identification. Addition of Pluronic F127 offers clear-cut separations of standard proteins up to a relative molecular mass of 5 x 10(4) Da and allows to reveal protein/polypeptide microheterogeneity where applicable. None of the systems tested is suitable for the separation of acidic polypeptides and polyproline.
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PMID:The effect of sodium dodecyl sulfate and Pluronic F127 on the electrophoretic separation of protein and polypeptide test mixtures at acid pH. 1211 32

Early plant defense response is characterized by elevation of activity of peroxidases and enhanced insolubilization of hydroxyproline-rich glycoproteins, such as extensin, in the cell wall. The insolubilization process (cross-linking between soluble extensin precursor molecules) is catalyzed by extensin peroxidases. We have ionically eluted extensin peroxidases from intact water-washed suspension-cultured tomato (hybrid of Lycopersicon esculentum Mill. and Lycopersicon peruvianum L. [Mill.]) cells and purified them to homogeneity by molecular sieve and cation-exchange chromatography. Four ionic forms of peroxidase (PI,PII,EPIII, and EPIV) were resolved; only the latter two cross-linked tomato soluble extensin. The molecular weight (34,000-37,000), amino acid composition, and isoelectric point (9.0) of the extensin peroxidases were determined. Substrate specificities of the enzymes were investigated: soluble extensin and potato lectin (a hydroxyproline-rich glycoprotein with a domain that strongly resembles extensin) were cross-linked by only two forms of the enzyme, whereas bovine serum albumin, aldolase, insulin, a number of other marker proteins, and proteins eluted from tomato cells (except extensin) could not be cross-linked. We have also isolated a yeast elicitor that enhances total peroxidase activity and extensin insolubilization within 1 h of challenge in cultured cells of tomato. A highly sensitive enzyme-linked immunosorbent assay technique using polyclonal antiserum raised against soluble tomato extensin was used to demonstrate extensin insolubilization in vivo. A tomato cell-wall peroxidase that cross-links extensin has been purified and may have a role in plant defense.
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PMID:Purification and Partial Characterization of Tomato Extensin Peroxidase. 1222 57

Freeze-induced perturbations of the protein native fold are poorly understood owing to the difficulty of monitoring their structure in ice. Here, we report that binding of the fluorescence probe 1-anilino-8-naphthalene sulfonate (ANS) to proteins in ice can provide a general monitor of ice-induced alterations of their tertiary structure. Experiments conducted with copper-free azurin from Pseudomonas aeruginosa and mutants I7S, F110S, and C3A/C26A correlate the magnitude of the ice-induced perturbation, as inferred from the extent of ANS binding, to the plasticity of the globular fold, increasing with less stable globular folds as well as when the flexibility of the macromolecule is enhanced. The distortion of the native structure inferred from ANS binding was found to draw a parallel with the extent of irreversible denaturation by freeze-thawing, suggesting that these altered conformations play a direct role on freeze damage. ANS binding experiments, extended to a set of proteins including serum albumin, alpha-amylase, beta-galactosidase, alcohol dehydrogenase from horse liver, alcohol dehydrogenase from yeast, lactic dehydrogenase, and aldolase, confirmed that a stressed condition of the native fold in the frozen state appears to be general to most proteins and pointed out that oligomers tend to be more labile than monomers presumably because the globular fold can be further destabilized by subunit dissociation. The results of this study suggest that the ANS binding method may find practical utility in testing the effectiveness of various additives employed in protein formulations as well as to devise safer freeze-drying protocols of pharmaceutical proteins.
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PMID:ANS fluorescence detects widespread perturbations of protein tertiary structure in ice. 1646 96

A novel packing for high performance gel filtration chromatography (GFC) was synthesized and characterized. High porosity silica prepared by base-dissolving method was used as the matrix. gamma-(2,3-Epoxy propoxyl) propyltrimethoxysilane was used as the ligand and covalently bonded onto the silica matrix. After acidic hydrolysis, the epoxy groups were converted to the diol groups. Because a condensation tube filled with water at 70 degrees C was used in the grafting reaction, the resulting methanol could easily be discharged from the reaction system to shift the reaction equilibrium to achieve high ligand density. The hydrolysis condition greatly affects ligand density and column efficiency. The high column efficiency is observed when the ligand density is between 2.6 and 3.5 +/- mol/m2. Several proteins, such as cytochrome C, chymotrypsin, ovalbumin, bovine serum albumin, aldolase, ferritin, insulin, gamma-globulin, phosphorylase, actin, carbonic anhydrase, were used to characterize the separation properties of the resulting high performance GFC column. It was shown that the excluded limit of relative molecular mass for the separation of bio-molecules was 300 000. The recovery yield of bovine serum albumin was 99%.
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PMID:[Synthesis and evaluation of high performance gel filtration chromatography packing of KH-s-GFC300]. 1649 90


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