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

Several aldolase B clones from a human liver cDNA library have been identified by using a rabbit aldolase A cDNA as a hybridization probe. The most complete of these, pHL413, is 1389 base pairs long and covers approximately equal to 80% of the length of the mRNA, including 90% of the translated region. The cDNA, pHL413, was used to identify a genomic clone, lambda HG313, which encoded the remaining amino acids of human aldolase B. We demonstrate that the amino acid and nucleotide sequences of aldolase are strongly conserved even between different isozymes. Furthermore, in the 3'-untranslated regions of the mRNAs for the B isozyme of human and rat there is an extensive stretch of homology. Aldolase B lacks a cysteine at positions 72 and 338 and lacks a histidine at position 361. These residues, which are present in rabbit aldolase A, have previously been proposed to take part in catalysis. Our findings suggest that this may not be the case.
 ...
PMID:Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones. 658 24

Hereditary fructose intolerance (HFI) is a disorder of visceral carbohydrate metabolism which is transmitted as a recessive character of moderate to high gene prevalence. The condition is caused by enzymic deficiency of aldolase B and is associated with the synthesis of inactive enzyme protein. The molecular structure of aldolase B was examined in tissue samples from four adult patients who were the offspring of non-consanguineous unions. Titration of aldolase protein, by radioimmunoassay, showed that antibody recognition of the inactive enzyme was attenuated differently in two unrelated HFI patients. The existence of separate structural lesions was confirmed by protein blotting and immunodetection of enzyme subunits after sodium dodecyl sulphate/polyacrylamide electrophoresis. In one patient the subunit size was identical to wild type (Mr 38,000) and in the other, a single faint band (Mr 39,000) was identified. Radioimmunotitration studies, in two affected offspring of this latter patient by a proven HFI carrier, also revealed differences in antibody recognition. Segregation of different mutant alleles within this kindred demonstrates heterogeneity in HFI occurring at the same genetic locus. Variations in apparent immunoreactivity of aldolase B in HFI are thus related to overt modification of enzyme subunits and indicate that the disorder results principally from structural rather than regulatory mutations in the aldolase B gene.
 ...
PMID:Allelic heterogeneity in adult hereditary fructose intolerance. Detection of structural mutations in the aldolase B molecule. 668 Jan 53

A solid-phase, noncompetitive radioimmunoassay has been developed for aldolase B in human serum and tissues. Aldolase B was purified from human liver, and specific antisera to purified aldolase B were obtained from chickens. Specific antihuman aldolase B IgG was purified by affinity chromatography. Disposable polypropylene plates were coated with affinity purified specific IgG antibody and used for radioimmunoassay with 125I-specific IgG antibody to aldolase B. The nonspecific binding was minimized by saturating the binding sites of the plates with 2% ovalbumin in 0.1% Tween 20. This radioimmunoassay is specific for the aldolase B subunit, with no cross-reactivity with human aldolase A or aldolase C subunits. Aldolase B is predominantly found in normal liver. Relatively high aldolase B levels are also observed in kidney. Serum levels of aldolase B in 21 normal subjects ranged from 21 to 39 ng per ml, with a mean of 28.7 +/- 8.6 (2 S.D.) ng per ml. Forty of 42 (95%) patients with acute and chronic hepatitis without cirrhosis had serum aldolase B levels greater than 40 ng per ml. Serum aldolase B levels correlated well with total serum aldolase enzyme activities (r = 0.967) and SGPT (r = 0.951) in patients with liver diseases. In cancer patients, serum aldolase B was slightly elevated in 15 of 26 (58%) patients with cancer metastatic to the liver or primary liver cell carcinoma, whereas no elevation of serum aldolase B was observed in 16 cancer patients without liver metastasis. Measurements of aldolase B serum levels by radioimmunoassay appear to be a useful measure of liver cell necrosis from benign or malignant liver diseases.
 ...
PMID:Human aldolase B serum levels: a marker of liver injury. 672 19

Hereditary fructose intolerance is due to a deficiency of liver aldolase (aldolase B). Little is known about its molecular mechanisms. We have tried to demonstrate the presence of the molecule and have explored the possibility of genetic heterogeneity. Liver samples from fifteen cases of hereditary fructose intolerance due to aldolase B deficiency were studied by various electrophoretic techniques. After electrophoresis on polyacrylamide gels, proteins were electrophoretically transferred on to nitrocellulose filters. They were treated with specific antialdolase B antibodies, and then with radioiodinated protein A, followed by autoradiography. Investigations included: (a) sodium dodecyl sulphate electrophoresis, in order to detect the presence of immunologically reactive molecules and to estimate the subunit size; (b) attempts to discover charge anomalies of the native molecule and of its subunits, by the use of: Isoelectric focusing of the native enzyme. Isoelectric focusing and non-equilibrium pH gradient electrophoresis (NEPHGE) after dissociation in urea. The major results were the following: (1) In all cases a cross-reacting material was found, with a molecular subunit size of 38000, indistinguishable from that of controls. (2) Evidence for molecular heterogeneity of the disease was provided by two types of data: amount of apparent immunologically reactive protein, which varied from less than 3% to 100% of that of controls; and charge data, aldolase B from seven patients showing an increased negative charge and from one patient a normal charge.
 ...
PMID:Molecular studies of liver aldolase B in hereditary fructose intolerance using blotting and immunological techniques. 676 Jul 89

Free ribosomes and membrane-bound ribosomes were prepared from rat livers, and the contributions of these two types of ribosomes to the synthesis of aldolase B were studied by the immunoprecipitation of [3H]puromycin-labeled nascent peptides with a rabbit antibody to this enzyme. Although rat liver aldolase was recovered in both cytosolic and microsomal fractions by the fractionation of liver homogenate, the microsomal aldolase was immunologically identical with its cytosolic counterpart as confirmed by Ouchterlony immunodiffusion test. We examined the nascent peptide fractions prepared from free and bound ribosomes, and found that the nascent peptides of aldolase were mainly localized in free ribosomes. About 0.5% of the total nascent peptides of free ribosomes and 0.08% of those of bound ribosomes was aldolase. The site of synthesis of serum albumin was also examined as a reference standard by the immunoprecipitation of labeled nascent peptides, and the nascent peptides of this secretory protein were mainly associated with bound ribosomes, as reported by other workers. These observations confirm that aldolase B is mainly synthesized by free ribosomes in rat liver cells.
 ...
PMID:Biosynthesis of aldolase B by free ribosomes in rat liver. 677 69

The influence of dexamethasone on the isozyme patterns of ATP-hexose phosphotransferases, aldolase and pyruvate kinase of adult rat hepatocytes maintained in primary cultures has been studied. A progressive loss of the typical adult liver isozymes glucokinase, pyruvate kinase L and aldolase B, with a simultaneous increase of both pyruvate kinase A and hexokinase activities, was observed in hepatocytes cultured in the absence of added glucocorticoid. When the culture medium was supplemented with 10(-7)M dexamethasone, the adult liver patterns of pyruvate kinase and aldolase were preserved for at least seven days of culture, the initial level of glucokinase was maintained for three days, and the rise of hexokinase activity was delayed and partially blocked. These results are discussed in relation to the known beneficial effect of glucocorticoids on the survival of cultured hepatocytes.
 ...
PMID:Effect of dexamethasone on the isozyme pattern of adult rat liver parenchymal cells in primary cultures. 711 Jan 29

A solid-phase, non-competitive radioimmunoassay for aldolase A in human serum has been developed. Human aldolase A was purified from muscle, and specific antisera to the purified aldolase A were obtained from chickens. Specific IgG anti-human aldolase A was purified by affinity chromatography. Disposable polypropylene plates were coated with specific IgG antibody and used for radioimmunoassay with 125I-specific IgG antibody to aldolase A. The non-specific binding was minimized by saturating the binding sites of the plates with 2% ovalbumin in 0.1% Tween 20. This radioimmunoassay is specific for the aldolase A subunit, with no cross-reactivity with human aldolase B subunit or homopolymeric human aldolase C(C4). The serum aldolase A immunoreactivities of 33 normal subjects ranged from 124 to 212 ng/ml with a mean of 178 +/- 41 ng/ml (+/- 2 SD). Ninety-three patients' sera were assayed with both a solid-phase non-competitive radioimmunoassay and a competitive double antibody radioimmunoassay developed in our laboratory and the results showed a high degree of correlation (r = 0.912; p less than 0.001). Rapidity and simplicity of the solid-phase assay makes it superior to other methods for the measurement of serum aldolase isozymes.
 ...
PMID:A non-competitive solid-phase radioimmunoassay for human aldolase A. 713 46

A radioimmunoassay was developed for the direct quantification of aldolase A in human serum. The method is a double antibody radioimmunoassay using radioiodinated aldolase A4 homopolymer as ligand, chicken antibodies to aldolase A, and rabbit antibodies to chicken IgG. The lowest measurable amount by this method was 2 ng (0.01 U). The radioimmunoassay was shown to be specific for the aldolase A subunit, with no cross-reactivity with human aldolase B subunits or homopolymeric human aldolase C (C4). The immunoreactive aldolase A in the sera of 41 normal healthy subjects ranged from 130 to 210 ng/ml (0.81-1.31 U/1), with a mean of 171 /+- 39 ng/ml.
 ...
PMID:Radioimmunoassay for human aldolase A. 731 82

Athletes in training have significantly higher levels of serum aldolase activity at rest when compared to nonathletes. This is due to the higher level (and higher proportion) of aldolase isoenzyme A, predominant in muscle. At rest, athletes with a history of infectious hepatitis show significantly higher proportional and absolute levels of aldolase B, predominant in liver. Long-lasting exercise leads to a rise in serum aldolase activity, which must be ascribed to the increase in isoenzyme A. Significant post-exercise changes in isoenzyme B were not observed. There was no correlation between changes in serum hemoglobin, as reflecting intravascular hemolysis, and changes in serum aldolase activity. The data are discussed in regard to the existing hypotheses regarding increases in serum enzyme activity after physical exercise.
 ...
PMID:Serum aldolase isoenzymes in athletes at rest and after long-lasting exercise. 733 33

Aldolases A and B (EC 4.1.2.13) and liver cytoplasmic superoxide dismutase (EC 1.15.1.1) have been purified from young and old dogs and mice. The specific activities of these enzymes were measured and show no diminution with age. In addition, dog aldolase B, dog liver superoxide, and mouse liver aldolase were titrated in crude extracts with specific antisera. No accumulation of cross-reacting material with age was detected. The electrophoretic mobilities of these enzymes and the susceptibilities of dog aldolases A and B to trypsin digestion were also unchanged. These results are additional evidence that the accumulation of inactive enzymes is not an invariable concomitant of aging.
 ...
PMID:Comparison of specific activities of enzymes from young and old dogs and mice. 744 26


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>