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At least 865 records · Page 48Linked to original sources
PubMed1987

Fructose-1-phosphate and fructose-1,6-bisphosphate aldolases in the small intestinal mucosa.

Reference values are presented for the activity of fructose-1-phosphate aldolase (F1PA) and fructose-1,6-bisphosphate aldolase (FBPA) in the small intestinal mucosa of 32 nonaffected children, 8 nonaffected adults and 2 children with hereditary fructose intolerance (HFI). The 96% confidence limits for F1PA in children are 1.55 to 43.0 u/g protein, completely distinct from the results of the two affected children (1.3 and less than 0.1 u/g protein). With fructose-1,6-bisphosphate as subtrate, the 96% confidence limits are 10 to 324 u/g protein and the values for the two affected children, 23.7 and 9.3 u/g. Among the nonaffected children two mucosal biopsies with F1PA activities less than 1.55 u/g were found. In one mucosal biopsy among the nonaffected children an FBPA activity less than 10 u/g was recorded. The data are interpreted as indicating that the determination of F1PA activity in intestinal mucosa is a highly sensitive test in detecting individuals with HFI. However, the specifity of the test is not absolute. Diagnosis should be based on both clinical and laboratory considerations. The determination of FBPA activity in the same biopsy specimen does not contribute substantially to the differential diagnosis.

Adult↗
PubMedDate not supplied

[Determination of aldolase A activity in the serum of patients with myocardial infarction].

A procedure is described for estimation of aldolase of the type A-a tissue-specific enzyme of myocardium--in blood serum under conditions of myocardial infarction. The rate of the enzymatic reaction was estimated by monitoring production of heptulose-1,7-diphosphate. Erythrose-4-phosphate and dihydroxyacetone phosphate were used as substrates of the reaction. High rates of the reaction product accumulation was observed if the compounds, shifting the reaction K'equi, were not added into the experimental samples. Sensitivity of the test was 3-fold increased due to modifications of the original method. Clinical experience with the test showed that activity of aldolase of the type A was distinctly higher in blood serum of patients with myocardium infarction as compared with the healthy donors or with the patients with ischemic heart disease.

Clinical Enzyme Tests↗
PubMed1985

The NADP binding site on rabbit muscle aldolase.

Rabbit muscle aldolase binds NADPH with a 1:1 stoichiometry and with a dissociation constant 18 microM. Three sites of the dinucleotide are involved in the binding: the adenosyl diphosphate moiety, the nicotinamide-ribose, and the nicotinamide ring. These data show the existence of a specific dinucleotide binding site in the aldolase molecule.

Animals↗
PubMedDate not supplied

Significance of serum phosphohexose isomerase, hexokinase and aldolase in carcinoma ovary.

The serum phosphohexose isomerase (PHI), aldolase and hexokinase activities have been determined in 36 patients of carcinoma ovary with different clinical stages and in 25 healthy normal female subjects. The serum PHI and hexokinase levels were significantly elevated (P less than .001) in all the stages of malignancy while serum aldolase was significantly elevated only in stages III and IV of malignancy. The enzyme levels showed statistically significant response to therapy in stage II patients. The mean values in patients with progression of the disease were not significantly different.

Female↗
PubMed1985

Structure of rabbit muscle aldolase at low resolution.

X-ray diffraction data were measured by x-ray diffractometry to 5-A resolution for both the monoclinic form of rabbit skeletal muscle aldolase (EC 4.1.2.13) and a platinum derivative. The heavy atom difference patterson was solved at 6-A resolution yielding eight distinct heavy atom sites. Choice was made of the enantiomorph and protein phases were calculated on the basis of single isomorphous replacement differences. The electron density map calculated from these phases was averaged according to the non-crystallographic molecular symmetry. Rotational symmetry analysis of native patterson and site symmetry analysis of refined heavy atom positions are consistent with the aldolase tetramer possessing a very high degree of 222 internal symmetry. The subunits in the tetramer are positioned in a tetrahedral configuration displaying a slight square planar deformation. Each subunit is roughly ellipsoidal in shape with the major axis nearly parallel to a local 2-fold axis. Prominent at the surface of each subunit were structural features resembling alpha helices. Each subunit contributes to its boundary surface at least six helices which are arranged in a barrel-like manner and possessing a right handed twist with respect to each other. Density associated with binding of substrate on the enzyme was located on the surface of each subunit. Cooperative aspects of the conformational changes produced upon substrate binding are discussed.

Animals↗
PubMed1977

Effects of life-long dietary protein restriction on mortality, growth, organ weights, blood counts, liver aldolase and kidney catalase in Balb/C mice.

Certain types of nutritional restriction can prolong life in mammals. This investigation documents life long effects of five protein diets in 1,000 Balb/c male mice. Balb mice subjected to 4% protein (lowest) diet had life expectancy that was marginally significantly prolonged when compared with control mice fed 24% protein (highest) diet. Body and organ weights of protein restricted mice generally were less than control mice. No significant differences among diets were found with blood counts, protein concentrations of liver and kidneys, or kidney catalase activity. Kidney catalase activity fell with age. Liver aldolase was induced by dietary sucrose, and aldolase fell with age in protein restricted mice, but not in controls.

Aging↗
PubMedDate not supplied

[Cadmium, zinc, pseudo-cholinesterase and aldolase blood levels in hypertensive and alcoholic patients. Preliminary statistical computerised study on 124 cases (author's transl)].

Changes in blood-level of cadmium, zinc, pseudocholinesterase and aldolase were studied in 44 normal subjects, 40 hypertensive patients and 40 alcoholic ones. The highest serum concentration of cadmium and pseudocholinesterase, the lowest serum and blood concentrations of zinc, the lowest serum concentrations of aldolase were found in the two groups of patients, with still lower levels in alcoholic patients than in hypertensive ones. There was a negative correlation between zinc and cadmium levels in the three groups of subjects. There was a high correlation between systolic and diastolic blood pressure value and cadmium, and negative correlation between blood pressure and zinc blood and serum levels.

Adult↗
PubMedDate not supplied

[Effect of insulin on the turnover of liver aldolase in irradiated rats].

A study was made of the effect of insulin on the rate of biosynthesis, "half life", spontaneous decomposition and transport of aldolase in mitochondria of liver and blood plasma of rats subjected to whole-body X-irradiation. The hormone injected after irradiation was shown to normalize the rate of spontaneous decay and the time of aldolase functioning.

Animals↗
PubMed1984

Catalytic activity of rabbit skeletal muscle aldolase in the crystalline state.

The monoclinic crystalline form of aldolase from rabbit skeletal muscle grown at 29 degrees C is catalytically active in the direction of aldol cleavage. Activity was assayed for in a crystallization buffer containing 45% saturated ammonium sulfate using chemically unmodified single crystals cut to precise dimensions. Diffusion effects on velocities from assays employing aldolase crystals do not appear to be limiting when cut single crystals are crushed. Assays of crushed crystals are linear with respect to both time and enzyme concentration. Kinetic constants are reported for both substrates fructose 1-phosphate and fructose 1,6-phosphate. Maximal velocities and binding constants determined differ by no more than a factor of 2 between the crystalline and the soluble state of the enzyme. Analysis of the kinetic constants for fructose 1-phosphate as substrate shows that binding of substrate does not change in going to the crystalline state. Release of product is reduced roughly 2-fold in the crystalline state. A similar conclusion can be reached in the case of fructose 1,6-phosphate as substrate provided the "on" steps of substrate and product are only diffusion limited but independent of the physical state of the enzyme. It is not possible to distinguish between a more sluggish conformational change during catalysis or simply tighter product binding in the crystalline state as compared to the soluble enzyme state.

Animals↗
PubMed1984

Anaerobic expression of maize fructose-1,6-diphosphate aldolase.

The anaerobic proteins of maize are a set of 10 major and 10 minor polypeptides selectively synthesized in anaerobic seedling roots. 1) Anaerobiosis resulted in the selected labeling of a protein which bound to Blue Sepharose and was eluted by fructose 1,6-diphosphate. 2) This protein elicited antiserum which recognized a single protein with molecular weight of approximately 40,000. 3) By Western blot analysis, this antiserum recognized a maize fructose-1,6-diphosphate aldolase purified to homogeneity. We show that two major anaerobic proteins of maize, ANP35.5 and ANP33A, correspond to a cytoplasmic fructose-1,6-diphosphate aldolase.

Anaerobiosis↗
PubMed1976

[Immunologic properties of fructose diphosphate aldolase in rabbit muscle under normal conditions and during fasting].

Methods of double diffusion failed to detect differences in immunological properties of aldolase from muscles of normal rabbits and those fasting for a long time. Therefore a quantitative method was used to inhibit the aldolase activity by homologous and heterologous antisera. The data obtained evidence for appearance of additional antigen determinants in an algolase molecule of the animals fasting for a long time; the determinants being sterically connected with the site of the enzyme active centre.

Animals↗
PubMedDate not supplied

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.

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.

Acid Phosphatase↗
PubMed1984

Evidence that aldolase and D-arabinose 5-phosphate are components of pentose pathway reactions in liver in vitro.

An immunochemical procedure involving the reaction of liver aldolase antibody and rat liver enzyme preparation shows that conversion of ribose 5-P to hexose 6-P by reactions of the non-oxidative pentose pathway fails to occur in the absence of aldolase activity. Radioautography of pentose pathway products formed by liver enzyme catalysis of [U-14C] arabinose 5-P and unlabelled ribose 5-P illustrates the incorporation of 14C into ketopentose, sedoheptulose, fructose and glucose phosphates. There is approximate congruity of the mole specific radioactivity of the pentose and hexose phosphates. These findings are consistent with the proposal that L-pentose pathway reactions constitute the non-oxidative segment of the pathway in liver.

Animals↗
PubMed1983

Mechanism of aldolase binding to erythrocyte membrane: Part II. Kinetic aspects.

The nature of binding of FDP aldolase to bovine erythrocyte membrane was examined. The Km value of bound and soluble enzyme differed by an order. The absence of time-lag in the velocity-time curves at various concentrations of the substrate and the similar extent of inactivation of bound and soluble enzyme on heat treatment suggested that the enzyme was bound at a point other than the catalytic site. The release of the enzyme by various glycolytic intermediates suggested their involvement in binding to the catalytic site through phosphate linkage. The non-phosphorylated compounds like lactate, reduced glutathione, 2-mercaptoethanol and EDTA were ineffective in eluting the enzyme. On the basis of separate binding sites on the enzyme for membrane and ligands, the mechanism of association dissociation of aldolase has been suggested.

Animals↗
PubMedDate not supplied

[Various properties of immobilized aldolase].

The pH dependence of direct and reverse aldolase reaction rate was studied in the presence of Sephadex-immobilized fructoso-1,6-diphosphate aldolase. The immobilized enzyme retains its activity in the presence of sulfhydryl inhibitors: iodacetate and n-chloromercury benzoate.

Animals↗
PubMed1978

Kidney in the aging cat: hexokinase, aldolase, L-alpha-glycerophosphate dehydrogenase, and lactate dehydrogenase histochemistry.

Hexokinase, aldolase, L-alpha-glycerophosphate dehydrogenase, and lactate dehydrogenase activities were determined in the kidney of the aging cat. Kidneys from 24 domestic cats 2 months to 7.5 years old in 6 age groups were examined by light microscopic and histochemical methods. Enzyme activities in anatomic components of the kidney were assessed on a quantitative basis for evaluation of mean activity between the age groups. In the cats with advancing age, renal components generally had stable activity. A significant (P less than 0.05) increase in hexokinase activity occurred with advancing age in the ascending part of the renal loop (Henle's loop) and in the distal convoluted tubule. Significant (P less than 0.05) increases in aldolase activity with aging were in cortical connective tissue, internal part of the glomerular capsule (podocytes), distal convoluted tubule, and convoluted segment (Pi) of the proximal portion of the nephron tubule. L-alpha-glycerophosphate dehydrogenase and lactate dehydrogenase activity increased significantly with aging in the convoluted (Pi) segment of the proximal portion of the nephron tubule.

Aging↗
PubMedDate not supplied

[Structural differences of C-terminal fragment of the alpha-subunits of rabbit muscle aldolase in normal animals and in experimental atherosclerosis].

The COOH-terminal BrCN fragment of the aldolase alpha-subunit from muscles of rabbits in norm and under atherosclerosis was studied by the method of dansyl-fingerprints in a silicagel and polyamide thin layer. It is shown that under atherosclerosis the amount of peptides in the fragment under study increases and the topography of two of them changes. The content of lysine, serine and valine enhances in it. The results evidence for structural differences in C-terminal fragment of aldolase alpha-subunits in muscles of rabbits in norm and under experimental atherosclerosis.

Amino Acids↗