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At least 19 recordsLinked to original sources
PubMed1984

Stability of quaternary structure and mode of dissociation of fructosediphosphate aldolase isoenzymes.

Using a highly sensitive "subunit exchange" assay, we have studied the relative strengths of interactions between different subunit types (A and C) of fructosediphosphate aldolase and have determined the mode of dissociation of aldolase tetramers in vitro. Interactions between C subunits within C4 tetramers were found to be considerably more resistant to disruption than were interactions between A subunits in A4 tetramers with regard to increasing concentrations of H+, OH-, or urea. Slight dissociation of A4 was also observed in 1.2 M magnesium chloride. These observations suggest that the quaternary structure of aldolase C4 is inherently more stable than that of aldolase A4. Also, the symmetrical heterotetramer A2C2 was found to be more resistant to urea-mediated dissociation than was the aldolase A4 homotetramer; this observation suggests that, even when in heteromeric combination, C subunits have a stabilizing influence on the quaternary structure of aldolase tetramers. In no case did we find evidence for a stable dimeric intermediate in the dissociation of aldolase tetramers to monomers. These observations are considered in terms of the tetrahedral arrangement of subunits in the aldolase tetramer. The general applicability of the subunit exchange assay described here for studying the subunit structure and mode of dissociation of oligomeric enzymes is discussed.

Animals↗
PubMedDate not supplied

[Content of the nonsaponifying substances in crystalline fructosediphosphate aldolase from the muscles of rabbits normally and in atherosclerosis].

The non-saponifying fraction was found in highly purified crystalline preparations of fructose diphosphate aldolase (EC 4.1.2.13). The amount of the non-saponifying substance in the aldolase of intact animals is different and depends not only on the degree of the enzyme purification. In the experiments when the non-saponifying residue was added to the incubation mixture it was found to produce no effect on the aldolase activity with the presence of fructose-1,6-diphosphate and fructose-1-phosphate. A decrease is observed in the activity of the crystalline preparations during their storage for four months which depends directly on the amount of the non-saponifying fraction in these preparations. The amount of the non-saponifying fraction in equally purified preparations of aldolase with experimental atherosclerosis is twice as low as compared to the norm. The non-saponifying residues of the fructose-diphosphate aldolase muscular preparations in the norm and with experimental atherosclerosis consist of two components, one of them being cholesterol, the chemical nature of the other component is not the same in the norm and with atherosclerosis.

Animals↗
PubMed1975

[Study of the fructosediphosphate aldolase and transketolase activity in the nystatin producer, Actinomyces noursei].

Activity of transketolase, an enzyme of the pentose cycle and fructosodiphosphataldolase, an enzyme of glycolisis was studied in the dynamics of development of the nystatin-producing organism and its inactive mutant under various conditions of their cultivation with a purpose of finding relation between the antibiotic production and general metabolism of Act. noursei. The transketolase activity of the organism was 2-4 times higher than that of the inactive mutant. Addition of 8000 Units/ml of nystatin to the medium markedly suppressed (50-100 per cent) the aldolase activity, however it had no effect on the transkelotase activity. Possibly the antibiotic accumulated in the mycelium played the role of a regulator of the activity of the enzymes, directing the metabolites along the hexosomonophosphate pathway of carbohydrate dissimilation.

Aerobiosis↗
PubMedDate not supplied

[Changes in fructosediphosphate aldolase and glucose-6-phosphate dehydrogenase activity after irradiation of animals with an absolute lethal dose of gamma rays].

A single total-body exposure of rats to gamma-rays in an absolutely lethal dose caused significant changes in the activity of fructosodiphosphate aldolase (ALD) and glucose-6-phosphate dehydrogenase (G-6-PDH) in the brain, liver, myocardium and skeletal muscles. The activity of ALD was mainly inhibited and that of G-6-PDH increased. Thus, the initial step of glycolysis was significantly inhibited and the key reaction of the pentose phosphate pathway enhanced in the irradiated body.

Animals↗