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)

1) The activities of 16 enzymes of glycolysis and of glutathione metabolism were determined in intact human red cell membranes (ghosts) which were prepared by hypotonic hemolysis. 2) Enzymes and hemoglobin of the ghosts were resolved by two toluene extractions. Only the four enzymes hexokinase, fructose-bisphosphate aldolase, glyceraldehyde-phosphate dehydrogenase and pyruvate kinase could not be released completely from the ghosts. 3) The residual membrane fraction, which was obtained after the toluene extraction of ghosts prepared at 30 imOsM, contained 0.02% of the original hemoglobin content of the red cell. Between 6.5 and 23% of the hemolysate activities of glyceraldehyde-phosphate dehydrogenase, phosphoglycerate kinase, pyruvate kinase and fructose-bisphosphate aldolase were detected in this fraction after mechanical disruption. 4) Sonication of intact ghosts increased the activities of fructose-bisphosphate aldolase, pyruvate kinase and phosphoglycerate kinase. 5) In "white" ghosts prepared at 5 imOsM phosphate buffer which contained 0.5% of the original hemoglobin the activities of fructose-bisphosphate aldolase and glyceraldehyde-phosphate dehydrogenase were detected at high levels. The activities of pyruvate kinase and phosphoglycerate kinase were low in these preparations. 6) The results indicate that one part of all enzymes is loosely attached to the inner surface of the membrane as is hemoglobin. A second part, the "cryptic enzyme activity", is available after resolving by toluene. A residual part of four enzymes is firmly bound to the membrane. Two of them (fructose-bisphosphate aldolase and glyceraldehyde-phosphate dehydrogenase) are oriented toward the inner surface of the membrane, whereas pyruvate kinase and phosphoglycerate kinase are hidden in the lipid core of the membrane.
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PMID:Organization of enzymes of glycolysis and of glutathione metabolism in human red cell membranes. 16 42

A neutral SH-dependent proteinase was isolated from bovine spleen by a slight modification of the previous method (1) and its action on some natural and synthetic substrates was studied. The activity of the enzyme was increased 2000--2500-fold as compared to that of the original extract. The enzyme hydrolyzed various histones (H1, H2a, H2b, H3), casein and protamine but did not split hemoglobin, serum albumin and 14C-tryptophane-labelled total protein from chicken embryos. The enzyme possessed neither collagenolytic nor elastase activity; it did not inactivate aldolase, hexokinase, glyceraldehyde phosphate dehydrogenase and glucose-6-phosphate dehydrogenase, which makes the enzyme different from cathepsin B1 and some other previously described proteinases. The enzyme did not split BAPA, BAEE, ATEE, Boc-Ala-ONP, Leu-beta-NA and some other peptides. The molecular weight of the enzyme was found to be about 15 000.
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PMID:[Isolation and properties of neutral SH-dependent proteinase from bovine spleen]. 43 66

210 male patients hospitalized for cardiac rehabilitation have been studied. As a result of age matching the sample was reduced to 190 patients: 72 patients with myocardial infarction, 90 patients with functional cardiovascular diseases, and 28 patients with angina pectoris. At the beginning and at the end of the 4 to 6 week rehabilitation program total lipids, cholesterol, triglycerides, phosphatides, GOT, GPT, LDH, HBDH, cholinesterase, aldolase, blood sugar, creatinine, electrolytes, hemoglobin, erythrocytes, leukozytes, and catecholamines were measured. In addition to the statistical comparison of the three groups and their specific change patterns, effects of body weight reduction and improvement of physical fitness were analyzed. The decrease of lipids is especially associated with weight reduction, whereas the decrease of enzyme activity and electrolyte concentration is accompanied as well with weight reduction as with the improvement of physical fitness.
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PMID:[Biochemical measures in cardiac patients: an analysis of change during rehabilitation (author's transl)]. 69 75

The effect of perfluorochemical (PFC) emulsion (25 w/v per cent of PFC concentration) on carbon monoxide poisoning was studied in rats exposed to 97 per cent O2 and three per cent CO. There was no significant difference in conversion rate of hemoglobin to carboxyhemoglobin (COHb) between PFC emulsion and saline groups. However, after re-exposure to pure oxygen, PFC emulsion group circulation reconverted to oxyhemoglobin (OXYHb) at a significantly faster rate than circulation in the control group. Survival time of rats was considerably affected by infusion of PFC emulsion and prolonged in proportion to increased injection dosage. Significant elevations in plasma glucose, lactate and aldolase levels and lactate/pyruvate ratio were found in the saline group and these levels remained well within normal range in the PFC emulsion group. These results indicate that PFC emulsion can function as an oxygen carrier in the presence of carbon monoxide and can deliver sufficient oxygen to peripheral tissues.
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PMID:Effect of perfluorochemical (PFC) emulsion on acute carbon monoxide poisoning in rats. 73 57

Osmotically hemolysed pigeon erythrocytes retain a considerable part of the total cell content of aldolase activity. After washing off the ghosts from hemoglobin and removing the nuclei, a considerable portion of aldolase activity is found in the supernatant. The retained part of aldolase is rather firmly bound to plasma membranes (PM), as evidenced by the fact, that double washing with a mixture of 0.3 M sucrose, 0.01 M tris-HCl (pH 7.4) and 0.004 M MgCL2, or with 0.15 M NaCl or H2O does not appreciably decrease the aldolase activity of PM. Only washing of PM with 0.5 M NaCl results in appreciable decrease of aldolase retention by PM. The binding of aldolase proved to be temperature sensitive: after heating the binding of aldolase to PM specifically decreased. These data suggest that the interaction of the enzyme with PM of pigeon erythrocytes occurs in the intact cell and may be of physiological significance.
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PMID:[Interaction of aldolase with pigeon erythrocyte plasma membranes]. 98 7

Tarsal degenerative joint disease (DJD) in 27 cattle was classified as primary or secondary based on age, joint conformation defects, faulty hindlimb alignment, or history of trauma to the affected joint(s). Results of blood and synovial fluid analysis for cattle affected with primary or secondary tarsal DJD were grouped in compilation of data. Cattle with tarsal DJD had significantly (P smaller than 0.01) reduced hemoglobin (Hb) content in comparison to that in control cattle. There was highly significant (P smaller than 0.001) reduction in packed cell volume (PCV). A significant difference was not determined for mean corpuscular hemoglobin concentration (MCHC) values of the 2 groups of cattle. Total white blood cell (WBC) counts closely paralleled each other, although mean proportion of neutrophils was significantly (P smaller than 0.05) greater in cattle affected with tarsal DJD, as were mean proportion of lymphocytes (P smaller than 0.02). Synovial fluid samples were analyzed for physical, biochemical, and cytologic properties. Statistical comparisons were made between values determined for arthritic cattle and control cattle. All samples from cattle with tarsal DJD were transudative. Opacity and flocculation were attributed to the presence of cartilaginous fragments and fibrils. There was significant correlation between increased relative viscosity (RV) and higher grades of mucinous precipitate quality (MPQ; r = +0.294, P smaller than 0.05) for all cattle. Mean alkaline phosphatase (ALP) activity for arthritic cattle was significantly (P smaller than 0.001) reduced, as was the mean activity for lactic dehydrogenase (LDH; P smaller than 0.05). The mean aldolase (ALD) activity for arthritic cattle was increased, whereas mean activity values for glutamic oxalacetic transaminase (GOT) and glutamic pyruvic transaminase (GPT) were reduced. Samples from arthritic cattle had reduced total leukocyte counts and significantly (P smaller than 0.05) increased proportion of macrophages in comparison to the values in control cattle.
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PMID:Tarsal degenerative joint disease in cattle: blood and synovial fluid changes. 114 40

The erythrocytes of 350 pigtailed macaques (Macaca nemestrina) were examined for electrophoretic variation of hemoglobin and 26 enzymes. Seven enzymes showed variation in more than 1% of individuals: phosphoglucose isomerase, phosphoglucomutase-1, soluble NADP-dependent isocitric dehydrogenase, peptidase A, peptidase C, 2,3-diphosphoglycerate mutase, and acid phosphatase. Variation with lesser frequency was found in soluble glutamic-oxalacetic transaminase, phosphoglycerate kinase, lactic dehydrogenase, and hemoglobin. Only eight samples were tested for esterase D, and one of these had a variant phenotype. Enzymes with no clear variation were adenylate kinase, adenosine deaminase, phosphofructokinase, hexokinase, pyruvate kinase, glyceraldehyde 3-phosphate dehydrogenase, aldolase, phosphoglycerate mutase, phosphopyruvate hydratase (enolase), phosphoglucomutase-3, and superoxide dismutase. There was father-to-son transmission of PGI, PGM-1, peptidase C, 6PGD, 2,3-DPGAM, NADP-ICD, and acid phosphatase variants, suggesting that these loci are autosomal as in man.
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PMID:Intraspecific red cell enzyme variation in the pigtailed macaque (Macaca nemestrina). 114 87

Studied were the changes in the values of some hematologic indices (hemoglobin, erythrocytes, leukocites) as well as the values of some biochemical (total protein and protein fractions, urea, total lipids, bilirubin, inorganic, phosphorus calcium) and enzyme factors (lactatedehydrogenase, alkaline and acid phosphatase, aldolase, amino transferrases, creatinephosphokinase) in geese prior to and after experimental infection of Borrelia anserina. It was found that in the peak stage of spirochetemia the content of hemoglobin, total lipids, and calcium, the percent of albumins and alfa-globulins, and the activity of the alkaline phosphatase in the blood decreased. The prealbumin fraction of the serum protein was completely reduced. The activity of the lactatedehydrogenase, acid phosphatase, amino transferrases, and aldolase showed higher values that were statistically significant, while the activity of the creatinephosphokinase rose to a slighter extent. The urea, bilirubin, inorganic phosphorus, and the alfa-, beta-, and gamma-globulins correlated positively with the course of the infection.
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PMID:[Biochemical changes in the blood of geese infected with Borrelia anserina]. 117 37

Hypotonic human erythrocyte ghosts, devoid of the original glyceraldehyde-3-phosphate dehydrogenase content of the red cell, bind added glyceraldehyde-3-phosphate dehydrogenases, isolated from human erythrocytes, rabbit and pig muscle, as well as rabbit muscle aldolase. There are only slight differences in the affinities towards the various glyceraldehyde-3-phosphate dehydrogenases. On the other hand, glyceraldehyde-3-phosphate dehydrogenases are bound much stronger than aldolase; in an equimolar mixture the former can prevent the binding of the latter, or replace previously bound aldolase at the membrane surface. Binding is always accompanied by the partial inactivation of enzymes, which can be reverted by desorption. Unwashed ghosts rich in hemoglobin seem to have a more pronounced inactivating effect on bound glyceraldehyde-3-phosphate dehydrogenase. In isotonic media ghosts, whether white or unwashed, reseal and do not interact with the enzymes.
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PMID:Partial reversible inactivation of enzymes due to binding to the human erythrocyte membrane. 126 75

The cytoplasmic domain of the human erythrocyte membrane protein, band 3 (cdb3), contains binding sites for hemoglobin, several glycolytic enzymes, band 4.1, band 4.2, and ankyrin, and constitutes the major linkage between the membrane skeleton and the membrane. Although erythrocyte cdb3 has been partially purified from proteolyzed red blood cells, further separation of the water-soluble 43-kDa and 41-kDa proteolytic fragments has never been achieved. In order to obtain pure cdb3 for crystallization and site-directed mutagenesis studies, we constructed an expression plasmid that has a tandemly linked T7 promoter placed upstream of the N-terminal 379 amino acids of the erythrocyte band 3 gene. Comparison of several Escherichia coli strains led to the selection of the BL21 (DE3) strain containing the pLysS plasmid as the best host for efficient production of cdb3. About 10 mg of recombinant cdb3 can be easily purified from 4 L of E. coli culture in two simple steps. Comparison of cdb3 released from the red blood cell by proteolysis with recombinant cdb3 reveals that both have the same N-terminal sequence, secondary structure, and pH-dependent conformational change. The purified recombinant cdb3 is also a soluble stable dimer with the same Stokes radius as erythrocyte cdb3. The affinities of the two forms of cdb3 for ankyrin are essentially identical; however, recombinant cdb3 with its unblocked N-terminus exhibits a slightly lower affinity for aldolase.
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PMID:Expression, purification, and characterization of the functional dimeric cytoplasmic domain of human erythrocyte band 3 in Escherichia coli. 130 97


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