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 ablity of competent and noncompetent Streptococcus sanguis (strain Wicky) cells to release enzymes to the environment was studied. Both competent and noncompetent cells leaked the enzymes tested (aldolase, phosphatase and deoxyribonuclease), but the activities liberated from the competent cells were always roughly 2-fold higher than those released from noncompetent cells. This increased enzyme leakage from competent cells occured in all kinds of media and procedures employed. The leakage of enzymes followed a time-dependent kinetics (different for aldolase and phosphatase), was temperature sensitive and had a pH optimum. The increased enzyme release was most likely not due to cell disruption, but seemed to be rather a consequence of alteration in cell barrier permeability. These results strongly support the "unmasking" model proposed for explanation of competence development in bacteria.
Acta Microbiol Pol 1978
PMID:Competence-related increased enzyme release from Streptococcus sanguis (Wicky) cells. 8 92

The binding isotherms of native bovine serum albumin with cationic detergents, such as octyl, decyl, dodecyl and tetradecylpyridinium bromides were determined at pH 6.8 and 3.4 at 25 degrees C. The isotherms for dodecyl and tetradecylpyridinium bromides were also determined at 3 degrees C. The average number of detergent cations bound increased with increasing hydrocarbon chain length. At low detergent concentration the binding of all alkylpyridinium bromides was smaller at pH 3.4 than at pH 6.8. Dodecylpyridinium bromide was bound to native beta-lactoglobulin, aldolase, ovalbumin, haemoglobin, myoglobin, lysozyme, trypsin and ribonuclease at pH 6.8. No binding occurred to alpha-chymotrypsin and chymotrypsinogen. The free enthalpy change, --delta G degrees, calculated from intrinsic association constants K was determined.
Acta Biochim Pol 1979
PMID:Protein-cationic detergent interaction. Equilibrium dialysis study of the interaction of bovine serum albumin and other proteins with alkylpyridinium bromide. 49 43

The influence of cysteamine on the metabolic activity of red blood cells has been estimated in vitro. Cysteamine has a marked influence on the activity of mainly aldolase F-1, 6-P and glucose-6-P dehydrogenase in red blood cells in vitro. The anaerobic metabolism of erythrocytes is more active in the presence of lower doses of cysteamine. Higher concentrations of radioprotector stimulate the pentose phosphate shunt.
Pol J Pharmacol Pharm 1976
PMID:The influence of the known radioprotective compounds on the metabolism of human red blood cell. Part II. The influence of cysteamine on enzymic systems. 93 45

In 200 patients with neuromuscular diseases the author studied malonic dehydrogenase and lactic dehydrogenase activity comparing it with the activity of serum creatine kinase and aldolase. A significant rise in the values of all these enzymes was found only in the Duchenne type of muscular dystrophy, in polymyositis, and less frequently in the limb-girdle type of muscular dystrophy. Raised activity of creatine kinase and sidolase was observed in mothers and sisters of patients with Duchenne type of dystrophy, in patients with non-progressive myopathy, periodic paralysis, amyotrophic lateral sclerosis and polyneuropathy. With progression of dystrophy the activity of these enzymes decreases.
Neurol Neurochir Pol
PMID:[Serum enzymatic activity in neuromuscular diseases]. 112 44

Structure of aldolase, its interaction with nucleotides, the path of enzyme reaction and the scheme of range of conformational changes of this enzyme are presented. Retrospectives and perspectives of aldolase topography investigations are included.
Acta Biochim Pol 1991
PMID:Topography and conformational changes of fructose-1,6-bisphosphate aldolase. 181 34

The site-specific modification of rabbit muscle aldolase A by labeling of thiol residues of Cys-289 with 5-(2-((iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid and Cys-239 with 5-iodoacetamidofluorescein or 4-dimethylamino-phenylazophenyl-4'-maleimide has been described. The method is based on the differences in kinetics of the chemical modification of aldolase thiols with the above reagents either in the presence or in the absence of a competitive inhibitor. The spectral properties of the doubly labeled aldolase derivatives were compared with those of the singly labeled enzyme. The doubly labeled aldolase derivatives exhibited full catalytic activity.
Acta Biochim Pol 1990
PMID:Site-specific modification or rabbit muscle aldolase with fluorescent probes. 212 52

The effect of Datura alba (seed) extract on the brain and urinary metabolites of rats was studied. Treatment with Datura brought about a decrease in the activity of brain lipid peroxidase and catalase while an increase in the activity of fructose diphosphate aldolase and glucose 6-phosphate dehydrogenase was observed. An increase in the DNA and RNA contents of brain was noted after the treatment with Datura. The study also showed a marked decrease in the excretion of 5-hydroxyindole acetic acid and vanillyl mandelic acid in the urine of rats given Datura extract.
Pol J Pharmacol Pharm
PMID:Effect of Datura (seed) on rat brain and urinary metabolites. 243 Feb 65

D-galactonate-grown cells of Mycobacterium sp. 607 can utilize D-galactonate by a pathway involving D-galactonate dehydratase, 2-keto-3-deoxy-galactonate kinase and 6-phospho-2-keto-3-deoxygalactonate aldolase. The enzymes have been separated by ion-exchange chromatography on DEAE-cellulose or ultrafiltration on Sephadex G-100. Partial characterization on the kinase and the aldolase have been described.
Acta Microbiol Pol 1983
PMID:Separation and some properties of D-galactonate pathway enzymes from Mycobacterium sp. 607. 619 65

Twenty Thoroughbred 3 year old horses (10 stallions and 10 mares), trained and raced at the Warsaw Race-Course were studied from March through November. Blood was taken approximately every 8 weeks to determine the activities of aspartate and alanine transaminases, acid and alkaline phosphatases and aldolase. It was observed that the activities of aspartate aminotransferase and alkaline phosphatase reached their maxima in July and alanine transaminase in May. The activities of acid phosphatase and aldolase showed their minima in July. Comparing these data with the literature it was noted that the changes observed are mainly seasonally-dependent; but, training had some influence on the activity of the enzymes involved in energy metabolism.
Acta Physiol Pol
PMID:Seasonal enzyme activity changes in two aminotransferases AspAT and AlAT, acid and alkaline phosphatases and aldolase in the serum of Thoroughbred horses during a racing season. 653 19

Phosphorylated fructose-1,6-bisphosphatase (FBPase) was isolated from rabbit muscle in an SDS/PAGE homogeneous form. Its dephosphorylation with alkaline phosphatase revealed 2.8 moles of inorganic phosphate per mole of FBPase. The phosphorylated FBPase (P-FBPase) differs from the dephosphorylated enzyme in terms of its kinetic properties like K(m) and k(cat), which are two times higher for the phosphorylated FBPase, and in the affinity for aldolase, which is three times lower for the dephosphorylated enzyme. Dephosphorylated FBPase can be a substrate for protein kinase A and the amount of phosphate incorporated per FBPase monomer can reach 2-3 molecules. Since interaction of muscle aldolase with muscle FBPase results in desensitisation of the latter toward AMP inhibition (Rakus & Dzugaj, 2000, Biochem. Biophys. Res. Commun. 275, 611-616), phosphorylation may be considered as a way of muscle FBPase activity regulation.
Acta Biochim Pol 2003
PMID:Rabbit muscle fructose-1,6-bisphosphatase is phosphorylatedin vivo. 1267 51


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