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)

Investigations were carried out with a total of 276 high-producing and clinically healthy cows that had freshly calved on 11 farms, being divided into groups according to the extent to which ketonuria was present if al all. Whole blood and blood serum were sampled to determine the ketone bodies, blood sugar, erythrocyte and leukocyte counts, hemoglobin, inorganic phosphorus, Ca, Mg, total protein, carotene, and activity of the GOT and GPT enzymes as well as the activity of lactic acid dehydrogenase, alkaline phosphatase, aldolase, and leucine aminopeptidase. Studied were the body temperature, the pulse rate, and the respiration rate. It was found that on farms with ketosis in cows ketonuria was manifested most often after the ketone bodies in the blood rose to 10-12 mg%. At the same time the blood sugar level was lowered and as a rule it showed reverse correlation with the levels of ketonemia and ketonuria. In such cows there was a lowering trend with the Ca and carotene contents and the erythrocyte count, and the respiration rate was higher. There were no changes in the body temperature, pulse rate, leukocyte count, Ca, Mg, hemoglobin, protein, and the activity of aldolase. The activity of the other enzymes mentioned was higher, and it correlated positively with the rise of ketonemia and ketonuria. With diseased cows the activity of alkaline phosphatase only was shown to be lower, negatively correlating with ketonuria.
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PMID:[Changes in the serum enzymes and clinical and clinico-biochemical indices of cows with subclinical ketosis]. 653 57

Cathepsin L was capable of destroying rabbit muscle aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) activity towards the substrate fructose 1,6-bisphosphate. The rate of loss of activity towards this substrate was stimulated (approx. 2-fold) by physiological concentrations of ATP and to a lesser degree by GTP, CTP, UTP, ADP and cyclic AMP, while PPi and Pi decreased the rate of inactivation. Other proteinases (cathepsin B, cathepsin D, trypsin and chymotrypsin) also decreased aldolase activity toward fructose 1,6-bisphosphate more rapidly in the presence of ATP and more slowly in the presence of Pi. Cathepsin L, at higher concentrations, was capable of inactivating aldolase activity towards fructose 1-phosphate and extensively degrading the enzyme; these reactions were not affected by ATP and Pi. The thermostability of aldolase was also unaffected by these ligands. ATP and Pi had no effect on the rates of hydrolysis of other proteins (hemoglobin, bovine serum albumin, casein and azocasein) by cathepsin L. These data indicate that the effects of ATP and Pi are due to interactions of these ligands with aldolase that make the enzyme more vulnerable to limited but not extensive proteolysis; these ligands do not directly affect cathepsin L activity.
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PMID:Inactivation of fructose-1,6-bisphosphate aldolase by cathepsin L. Stimulation by ATP. 669 88

Hemoglobin, aldolase and glyceraldehyde 3-phosphate dehydrogenase are known to bind to the cytoplasmic domain of band 3 protein. Binding of glycolytic enzymes to band 3 protein is inhibited by its amino-terminal fragments. To precisely localize the sequence portion of band 3 protein to which hemoglobin binds and to see whether the same region of amino-acid sequence binds both hemoglobin and glycolytic enzymes, a simple, direct solid-phase binding assay was developed. Peptides generated from the 23-kDa fragment by trypsin, cyanogen bromide and mild acid hydrolysis were used as inhibitors to determine the minimal sequence structure involved in the binding of the 23-kDa fragment to hemoglobin. The shortest peptide which inhibits the binding of the 23-kDa fragment is an acid cleavage peptide containing the sequence positions 1 to 23. This sequence is unusual as 14 of its residues are negatively charged, it contains no basic residues and has its amino terminus blocked. Using aldolase, glyceraldehyde-3-phosphate dehydrogenase and hemoglobin as competitive inhibitors in the binding of 23-kDa fragment, the affinity of hemoglobin to this fragment appears several-fold weaker than that of both the enzymes. These findings demonstrate that glycolytic enzymes and hemoglobin bind competitively to the same polyanionic sequence region of band 3 protein.
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PMID:Hemoglobin binds to the amino-terminal 23-residue fragment of human erythrocyte band 3 protein. 671 38

Two SH-dependent proteinases (I and II) active in neutral media were isolated from bovine spleen and purified to apparent homogeneity. The histone-hydrolyzing activity of proteinase I was increased 3500-fold as compared to that of the original extract. Proteinase I hydrolyzed a variety of proteins (histones, azocasein, hemoglobin, collagen) but did not hydrolyze low molecular weight synthetic substrates, such as BAPA, BANA, BAEE, ATEE, Leu-beta-NA, Arg-beta-Na and Ala-beta-NA. The molecular weight of the enzyme as determined by SDS electrophoresis was found to be about 23,000. Isoelectrofocusing of the enzyme resulted in one major component with pI of 6.05 and in two minor components with pI of 6.2 and 6.4. Proteinase II hydrolyzed Leu-beta-NA, Arg-beta-NA and Ala-beta-NA but did not hydrolyze beta-naphthylamides of dicarboxylic acids and Gly-Phe-beta-Na. This proteinase split BANA and histone and very slowly split azocasein and collagen. Proteinase II was found to have a molecular weight of 30 000 and a pI of 6.8-6.9. Proteinase I inactivated fructose-1.6-diphosphate aldolase, partly inactivated glucose-6-phosphatase dehydrogenase and caused activation of phosphodiesterase of cyclic nucleotides. Proteinase II had no effect on the activity of the above enzymes. A comparison of proteinase I and II with enzymes described in literature demonstrated that the former was cathepsin L, while the latter was cathepsin H from spleen.
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PMID:[Characteristics of two thiol proteinases from spleen active in neutral media]. 675 12

We have synthesized diisethionyl-3,3'-dithiobispropionimidate (DIDIT), a new membrane-impermeant, cleavable protein cross-linking reagent designed for probing protein organization at one face of a membrane. Rabbit muscle aldolase were reacted in solution with DIDIT and the products were electrophoresed in sodium dodecyl sulfate-polyacrylamide gels. When electrophoresed under nonreducing conditions, the gels contain bands corresponding to oligomers of aldolase, while pretreatment with dithiothreitol to cleave the cross-link prior to electrophoresis results in gels containing primarily the band corresponding to aldolase monomer. These experiments demonstrate that DIDIT is a cleavable protein cross-linker. Reaction of isolated human erythrocyte membranes with DIDIT leads to extensive cross-linking of spectrin, band 3, and band 6, and residual hemoglobin, consistent with results previously obtained with permeant cross-linkers. In contrast, when intact human erythrocytes are cross-linked with DIDIT, hemoglobin and the cytoplasmic face membrane proteins are not cross-linked, but band 3, which is accessible at the extracytoplasmic face of the membrane, is cross-linked to dimers.
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PMID:A membrane-impermeant, cleavable cross-linker. Dimers of human erythrocyte band 3 subunits cross-linked at the extracytoplasmic membrane face. 724 Jan 79

Experiments were carried out with pigs in the course of 30 days with the use of dietary mixtures containing 10 and 20 per cent cultures of Fusarium tricinctum in rice. The treated animals showed higher sensitivity to trichotecenes. These moulds metabolites raised the activity of the serum glutamate oxaloacetate and glutamate-pyruvate transaminases, aldolase, lactate dehydrogenases, alkaline phosphatase, lipid level, and leukocyte count but lowered the amount of total protein and that of hemoglobin. The morphologic lesions seemed confined mainly to the stomach, intestines, and kidneys.
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PMID:[Clinical, morphological and biochemical changes in pigs caused by the toxic metabolites of Fusarium tricinctum]. 732 75

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.
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PMID:Serum aldolase isoenzymes in athletes at rest and after long-lasting exercise. 733 33

The isozyme patterns of glycolytic enzymes of Friend leukemia cells (FLC) were compared with those of erythrocytes and erythroblasts. Erythrocyte-specific R types of pyruvate kinase (PK) were clearly observed in phenylhydrazine-induced mouse erythroblast, and much less amount of them was also observed in Friend leukemia cells. When FLC were induced to differentiate by hexamethylene-bisacetamide (HMBA), the R types were slightly reduced. When the induction of differentiation was inhibited by 12-O-tetradecanoylphorbol 13-acetate (TPA), the R types and M2-R hybrids rather increased. These results are reverse of those obtained when hemoglobin production is used as a marker of differentiation. Isozyme patterns of lactic dehydrogenase and aldolase did not change during differentiation of FLC induced by HMBA, and were the same as those of mouse erythroblasts and erythrocytes.
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PMID:Isozyme patterns of pyruvate kinase and differentiation of Friend leukemia cells. 738 Jan 33

The major anion exchanger in type A intercalated cells of the cortical and medullary collecting ducts of the human kidney is a truncated isoform of erythrocyte band 3 (AE1) that lacks the N-terminal 65 residues. Because this missing sequence has been implicated in the binding of ankyrin, protein 4.1, several glycolytic enzymes, hemoglobin, and hemichromes in erythrocytes, we have undertaken examination of the structure and peripheral protein interactions of this kidney isoform. The cytoplasmic domain of kidney band 3, kidney CDB3, was expressed in Escherichia coli and purified to homogeneity. The kidney isoform exhibited a circular dichroism spectrum and Stokes radius similar to its larger erythrocyte counterpart. Kidney CDB3 was also observed to engage in the same conformational equilibrium characteristic of erythrocyte CDB3. In contrast, the tryptophan and cysteine clusters of kidney CDB3 behaved very differently from erythrocyte CDB3 in response to pH changes and oxidizing conditions. Furthermore, kidney CDB3 did not bind ankyrin, protein 4.1, or aldolase, and expression of erythrocyte CDB3 was toxic to its bacterial host, whereas expression of kidney CDB3 was not. Taken together, these data suggest that the absence of the N-terminal 65 amino acids in kidney CDB3 eliminates the major function currently ascribed to CDB3 in erythrocytes, i.e. that of peripheral protein binding. The primary function of residues 66-379 found in kidney CDB3 thus remains to be elucidated.
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PMID:Partial characterization of the cytoplasmic domain of human kidney band 3. 762 93

Aldolase deficiency of red blood cell is a rare cause of hereditary hemolytic anemia and now there exists only three patients in the world. We had a 24-year-old man operated on for gallbladder stone secondary to this uncommon disease. He underwent a cholecystectomy under general anesthesia combined with thoracic epidural block, using isoflurane, fentanyl, vecuronium, midazolam and lidocaine. During the surgery serum concentrations of bilirubin, free hemoglobin and LDH showed no change, suggesting a lower incidence of drug-induced hemolysis in the case of aldolase deficiency than in other enzyme deficiency. This fact also provides a useful guide to the choice of anesthetics and related agents. In the postoperative period, however, we found a hemolytic response to fever with a drop in hemoglobin level to 2.5 g.dl-1. Aldolase activity of his red cell is heat labile and an increase in body temperature may aggravate a disturbance in the glycolytic pathway leading to hemolytic crisis. It is thus important to prevent the body temperature from rising when a patient is suffering from hemolytic anemia due to red cell aldolase deficiency.
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PMID:[Anesthesia for a patient with red cell aldolase deficiency]. 851 55


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