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 sensitive new method in which D-[U-14C]fructose-1-phosphate is used for fructose-bisphosphate aldolase (EC 2.1.2.13) assay is described. The radioactive fructose-1-phosphate compound was prepared from [U-14C]fructose by use of partly purified fructokinase (EC 2.7.1.4). With this method we measured normal values for aldolase in human liver (2.4-10.0 nmol/min per mg of protein), kidney (3.6-3.8), and intestine (4.2-10.0) as well as Km values for fructose-1-phosphate (approximately 1.0-2.2 mmol/L). In patients with hereditary fructose intolerance the aldolase activity in liver and intestine was less than 10% of normal values. The Lineweaver-Burk plots for data from patients with hereditary fructose intolerance were hyperbolic, indicating a structural alteration in the enzyme.
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PMID:A radioisotopic method for fructose-1-phosphate aldolase assay that facilitates diagnosis of hereditary fructose intolerance. 662 33

The effect of wheel running on the levels of fructose 1,6-bisphosphate aldolase A (EC 4.1.2.13) in striated muscles of young and old mice was compared. Short-term (6-10 weeks) and long-term (over 12 months) regimens were included in the study. The studies were conducted on the CW-1 outbred strain and on the C57/BL inbred strain of mice. It was shown that, in the short-term regimens, old animals of both strains showed either no increase (C57/BL) or a reduction (CW-1) in aldolase activity in hind leg muscles. On the other hand, young animals of both strains showed increases in aldolase activity of 10-20%. In the long-term regimen young and intermediate age animals showed 30-100% increases in aldolase activity in hind leg muscles over control sedentary animals. This adaptive capacity to exercise was not observed in old animals. However, long-term exercise regimen prevented the age-associated decline in aldolase activity found in sedentary animals.
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PMID:The effect of short- and long-term exercise on aldolase activity in muscles of CW-1 and C57/BL mice of various ages. 665 9

Perfused rat hearts show a markedly increased binding of phosphofructokinase and fructose-bisphosphate aldolase as a consequence of ischaemia, but little change in binding of pyruvate kinase, lactate dehydrogenase or glyceraldehyde-3-phosphate dehydrogenase. After 10 min ischaemia over one quarter of the phosphofructokinase and three quarters of the aldolase are bound. The effect of anoxia is less well marked in its influence on binding with only aldolase showing a significant increase in binding. These results suggest that one factor involved in the increased binding during ischaemia is the fall in pH of the heart. Binding studies with isolated myofibrils confirm that the affinity and stoichiometry of aldolase binding are considerably increased as the pH is lowered over a range comparable to that which occurs in ischaemic heart. The low level of binding of glyceraldehyde-3-phosphate dehydrogenase in perfused rat hearts correlates with the relatively low affinity of this enzyme for binding to rat or rabbit cardiac myofibrils. There are species differences in the enzyme binding response to ischaemia. Sheep hearts show rapid and large increases in the binding of glyceraldehyde-3-phosphate dehydrogenase in addition to changes in aldolase and phosphofructokinase binding. The greater binding of glyceraldehyde-3-phosphate dehydrogenase reflects the greater affinity of sheep cardiac myofibrils. It is suggested that the altered metabolic demands of ischaemia are satisfied by changes in glycolytic enzyme organisation as the enzymes shift from the soluble to the particulate phase of cardiac muscle.
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PMID:Metabolic dependence of glycolytic enzyme binding in rat and sheep heart. 669 39

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.
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PMID:Human aldolase B serum levels: a marker of liver injury. 672 19

Highly purified glycosomes were isolated from Trypanosoma brucei bloodstream forms and cultured procyclic trypomastigotes. A comparison of the specific activities of glycosomal enzymes revealed that glycosomes from insect stages had decreased levels of hexokinase, phosphoglucose isomerase, phospho-fructokinase, fructose-bisphosphate aldolase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase, but contained increased levels of adenylate kinase, malate dehydrogenase and phosphoenolpyruvate carboxykinase. Glycosomes from bloodstream forms were almost totally devoid of the latter two activities. Comparison of the two types of glycosomes by sodium dodecylsulphate-polyacrylamide gel electrophoresis revealed that bloodstream form glycosomes contained 3 prominent polypeptides (64, 46 and 40 kDa) which were hardly detectable in insect stage glycosomes, whereas the latter contained 3 insect stage specific bands with molecular weight of 34 000, 61 000 and 77 000 and 4 additional bands with molecular weights between 94 000 and 110 000. Both types of glycosome contained the phospholipids phosphatidylcholine and phosphatidylethanolamine. Insect stage glycosomes contained in addition also phosphatidylinositol and some phosphatidylserine.
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PMID:A comparison of the glycosomes (microbodies) isolated from Trypanosoma brucei bloodstream form and cultured procyclic trypomastigotes. 674 87

The localization of a fetal isoenzyme of aldolase (A) in rat liver cells early after a single injection of carcinogen 4-dimethylaminoazobenzene and its noncarcinogenic analog 4-diethylaminoazobenzene has been studied using the immunofluorescent method. Aldolase A was found in the cytoplasm of oval and "transition" cells. These cells appeared in rat liver as a result of treatment with carcinogen and its analog. In mature hepatocytes aldolase A was not found either in intact rat liver, after the treatment with carcinogen or its analog.
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PMID:[Localization of embryonic aldolase isoenzyme in rat liver cells after a single injection of the carcinogen, 4-dimethylaminoazobenzene, and its noncarcinogenic analog]. 677 94

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.
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PMID:A non-competitive solid-phase radioimmunoassay for human aldolase A. 713 46

Ultraviolet difference spectra produced by the binding of mononucleotides and phosphates to rabbit aldolase A and B were analyzed. Both isozymes exhibit a distinct mode of interaction with the ligands. The binding seems to be based on multipoint interaction of nucleotides with each aldolase, indicating the existence of specific nucleotide binding domains in both proteins.
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PMID:Spectral evidence for distinct mode of interaction of nucleotides with rabbit muscle and rabbit liver aldolase. 721 98

S-Carboxymethylated chicken muscle aldolase was treated with cyanogen bromide to cleave the 4 methionyl bonds per subunit. Five homogeneous fractions were obtained designated fragments I-V. Fragment I was derived from the N-terminus and fragment II from the C-terminus of the enzyme. Reduction of the enzyme with NaB3H4 in the presence of dihydroxyacetone phosphate decreases the enzymatic activity by 90%. Fragment III contained the Schiff base-forming lysine residue since more than 83% of the radioactivity introduced by NaB3H4 reduction of aldolase-dihydroxyacetone phosphate was found in this fraction. A tryptic peptide of 27 amino acid residues containing the substrate-binding site was isolated. The gross molecular structure of aldolase A from chicken muscle indicates a high degree of homology with mammalian muscle aldolases.
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PMID:Studies on the structure of aldolase A from chicken muscle. 721 8

The intralysosomal localization of the enzymes that catalyse inactivation of rat liver fructose-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) to a form with antigenic activity was demonstrated. The inactivating enzymes like all other lysosomal markers tested except acid phosphatase, were readily solubilized by hypotonic shock. The inactivating enzyme activity was inhibited by PMSF, TPCK, TLCK and leupeptin, but not by pepstatin. On partial purification of the inactivating activity from the lysosomal fraction by DEAE-Sephadex (A-50) and Sephadex G-100 column chromatographies, it was copurified with lysosomal carboxypeptidase A and cathepsin B (EC 3.4.22.1). Studies on its substrate specificity and sensitivity to inhibitors indicated that cathepsin B and carboxypeptidase A are responsible for almost all the aldolase-inactivating activity in the lysosomal fraction.
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PMID:Properties of fructose-1,6-bisphosphate aldolase inactivating enzymes in rat liver lysosomes. 726 Jan


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