Wyniki wyszukiwania

1

The effect of metal ions and metabolites on the activity of pyruvate kinase from bean roots

100%

Jezewska M. J., Flieger M.

Applied Biology Communications. Lublin Scientific Center

|

1992

|

tom 02

|

nr 4

2

The synthesis of inorganic phyrophosphate from ATP and orthophosphate catalyzed by pyruvate kinase from heart and skeletal muscle

86%

Baranowska B., Baranowski T.

Bulletin of the Polish Academy of Sciences. Biological Sciences

|

1989

|

tom 37

|

nr 7-9

3

Pyruvate kinase in roots of germinating seeds of legumes. The comparison of plants transporting amides and ureides

86%

Jezewska M. J.

Applied Biology Communications. Lublin Scientific Center

|

1994

|

tom 04

|

nr 3-4

4

Comparison of pyruvate kinase variants from rat liver and Morris hepatoma 7777, obtained by an affinity chromatography on Blue Sepharose CL-6B

86%

Ignacak J., Guminska M.

Acta Biochimica Polonica

|

1993

|

tom 40

|

nr 2

Fractions A (salted out by ammonium sulphate between 21 - 30% saturation), and fractions B (salted out between 51 - 70% saturation) of pyruvate kinase (EC 2.7.1.40.) corresponding respectively to pyruvate kinase types L and M2 from rat liver and Morris hepatoma 7777 were purified by an affinity chromatography on Blue Sepharose CL-6B. Peaks of inactive proteins were eliminated and the enzyme fractions bound biospecifically to the gels were eluted by free ADP. The molecular mass of purified hepatoma pyruvate kinase fraction B was smaller than that of liver pyruvate kinase fraction B. Morris hepatoma pyruvate kinase fraction B represented a variant of type M2, characterised by greatest affinity to 2-phosphoenolpyruvate as a main substrate and different sensitivity to low-molecular effectors in comparison with types L from both liver and hepatoma and in comparison with type M2 from normal rat liver. Only this hepatoma fraction B showed a tumour specific sensitivity to L-cysteine and was insensitive to normal signal molecules i.e. to ATP and fructose-l,6-diphosphate which influence liver pyruvate kinase activity. L-Cysteine inhibited the tumour fraction B of pyruvate kinase by decreasing its Vmax and increasing the Km values in relation to 2-phosphoenolpyruvate.

5

Influence of salt on the activity of pyruvate kinase from yellow lupine root nodules

86%

Jezewska M. J.

Applied Biology Communications. Lublin Scientific Center

|

1992

|

tom 02

|

nr 2

6

Heart pyruvate kinase catalyses the synthesis of ATP from ADP and inorganic pyrophosphate

72%

Baranowska B., Baranowski T.

Bulletin of the Polish Academy of Sciences. Biological Sciences

|

1987

|

tom 35

|

nr 1-3

7

Tumor-specific pyruvate kinase isoenzyme M2 involved in biochemical strategy of energy generation in neoplastic cells

72%

Guminska M., Ignacak J., Kedryna T., Stachurska M. B.

Acta Biochimica Polonica

|

1997

|

tom 44

|

nr 4

The differences in properties of pyruvate kinase (EC 2.1.7.40) from normal tissues and animal or human tumors are described and their significance for various metabolic abnormalities is reviewed. The tumor variant gamma3 from M2 isoenzyme of pyruvate kinase sensitive to L-cysteine inhibition, when over-expressed, can be used as a marker of tumorigenic transformation. It seems that this variant represents a tumor-specific oncoprotein, involved in a novel metabolic strategy of energy generation during increased cell proliferation.

8

Changes in ATP level and iron-induced ultra-weak photon emission in bull spermatozoa, caused by membrane peroxidation during thermal stress

72%

Guminska M., Kedryna T., Laszczka A., Godlewski M., Slawinski J., Szczesniak-Fabianczyk B., Kwiecinska T., Rajfur Z., Wierzuchowska D.

Acta Biochimica Polonica

|

1997

|

tom 44

|

nr 1

ATP level, cell motility and viability, oxygen uptake, pyruvate kinase activity, and ultra-weak photon emission (UPE) induced by red-ox Fe2+ -ascorbate cycling system were studied in fresh, in previously equilibrated in a glycerol diluent, and in cryopreserved bull spermatozoa, exposed to thermal stress by incubation of the cells at 44°C. A sharp drop in motility and viability of fresh spermatozoa and even more so, of equilibrated and cryopreserved cells was accompanied by accumulation of ATP. When cell movement was totally inhibited, ATP utilization was decreased, while chemical energy continued to be produced by cell pyruvate kinase, one of the key glycolytic enzymes, which in spermatozoa is very active (6500 IU/g protein) and insensitive to feed-back inhibition by excess of ATP and I.-cysteine. Accumulation of ATP during incubation at 44°C in 0.9% NaCI was accompanied by a rapid decrease in oxygen consumption by fresh spermatozoa and an increase in Fe2+-ascorbate induced UPE, followed by a sharp decrease in ATP level observed at the end of induced UPE measurement. The increase in photon emission due to lipid peroxidation was highly correlated with the increase in cell ATP level caused by thermal stress.

9

Biochemical changes associated with Brassica juncea seed development. I. Respiratory enzymes

72%

Saroop S., Chanda S. V., Singh Y. D.

Acta Physiologiae Plantarum

|

1996

|

tom 18

|

nr 4

10

Pyruvate kinase of the heart muscle of the cockroach Periplaneta americana L.[Insecta: Blattodea]

58%

Lesicki A.

Bulletin de la Societe des Amis des Sciences et des Lettres de Poznan. Seria D: Science Biologiques

|

1994

|

tom 30

11

N-acetylneuraminic acid, phosphate and thiol groups of pyruvate kinase isoenzymes from Morris hepatoma 7777 and normal rat liver

58%

Ignacak J., Guminska M.

Acta Biochimica Polonica

|

1997

|

tom 44

|

nr 2

The highest amount of N-acetylneuraminic acid (AcNeu) was found in pyruvate kinase isoenzyme L from normal rat liver (24 moles/mole of enzyme tetramer), with the highest electrophoretic mobility. On the other hand, isoenzyme M2 from Morris hepatoma 7777, with the lowest electrophoretic mobility, had the lowest AcNeu content (5 moles/mole of enzyme tetramer). This tumour isoenzyme M2 of pyruvate kinase was, however, characterised by the highest phosphate content (12 moles/mole protein), in comparison to isoenzyme L (3 moles/mole protein) or normal liver isoenzyme M2 (6 moles/mole protein). This could indicate a regulatory change caused by reversible enzyme phosphorylation and dephosphorylation or sialization and desialization. Despite these differences, the sum of the two negatively charged residues was lower in tumour pyruvate kinase isoenzyme M2, with the slowest migration rate, than in normal rat liver isoenzyme M2. Moreover, isoenzyme M2 from tumour material, in comparison with isoenzyme M2 from normal rat liver, had a twice as high content of thiol groups (20 moles/mole protein), especially of free and superficially located ones, than the isoenzyme M2 from normal liver (10 moles/mole protein). This may explain abnormal susceptibility of tumour isoenzyme M2 to stereospecific inhibition by exogenous L-cysteine, and indicate genetically dependent changes in amino-acid content of tumour enzyme which take place during cell tumourigenic transformation.

12

Amino-acid composition of pyruvate kinase M2 isoenzyme variants from rat liver and Morris hepatoma 7777

58%

Ignacak J., Guminska M., Steczko J.

Acta Biochimica Polonica

|

1998

|

tom 45

|

nr 3

Cytosolic fractions B (salted out between 51-70% ammonium sulphate saturation) from rat liver and Morris hepatoma 7777, containing pyruvate kinase (EC 2.7.1.40) M2 isoenzymes, were purified by affinity chromatography on Blue Sepharose CL-6B. When compared by polyacrylamide gel electrophoresis at pH 8.3, all three M2 pyruvate kinase variants from Morris hepatoma 7777 had lower mobilities (α2, β2, γ3) than the three corresponding variants (α1, β1, γ2) from normal rat liver. Using an automatic amino-acid analyser, significant differences in selected amino- acid content have been found in corresponding highly purified γ3 and γ2 variants from Morris hepatoma and normal rat liver, respectively. The γ3 -variant of the Morris hepatoma M2 isoenzyme had twice the amount of L-tyrosine and L-cysteine, and a content of L-serine higher by 20% than the corresponding γ2 variant of the normal rat liver M2 isoenzyme. It contained, however, significantly less dicarboxylic amino acids which explains its lower electrophoretic mobility. It showed also a decrease (by ca. 10%) in several other amino-acid content, corresponding to a 10% decrease in the tumour enzyme molecular mass.

13

Kinetic properties of phosphofructokinase and pyruvate kinase in the midgut gland and abdominal muscle of the crayfish Orconectes limosus Raf. [Crustacea: Decapoda] after injections of 20-hydroxyecdysone

58%

Lesicki A.

Biological Bulletin of Poznań

|

1994

|

tom 31

14

Pyruvate kinase - a key enzyme of glycolysis in the tissues of selected snails of Poland

51%

Rybska E., Lesicki A.

Folia Malacologica

|

1998

|

tom 06

|

nr 1-4

15

Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik

Effect of high-protein diet on glycolytic processes in skeletal muscles of exercising rats

44%

Luczak-Szczurek A., Flisinska-Bojanowska A.

Journal of Physiology and Pharmacology

|

1997

|

tom 48

|

nr 1

Ograniczanie wyników

The effect of metal ions and metabolites on the activity of pyruvate kinase from bean roots

The synthesis of inorganic phyrophosphate from ATP and orthophosphate catalyzed by pyruvate kinase from heart and skeletal muscle

Pyruvate kinase in roots of germinating seeds of legumes. The comparison of plants transporting amides and ureides

Comparison of pyruvate kinase variants from rat liver and Morris hepatoma 7777, obtained by an affinity chromatography on Blue Sepharose CL-6B

Influence of salt on the activity of pyruvate kinase from yellow lupine root nodules

Heart pyruvate kinase catalyses the synthesis of ATP from ADP and inorganic pyrophosphate

Tumor-specific pyruvate kinase isoenzyme M2 involved in biochemical strategy of energy generation in neoplastic cells

Changes in ATP level and iron-induced ultra-weak photon emission in bull spermatozoa, caused by membrane peroxidation during thermal stress

Biochemical changes associated with Brassica juncea seed development. I. Respiratory enzymes

Pyruvate kinase of the heart muscle of the cockroach Periplaneta americana L.[Insecta: Blattodea]

N-acetylneuraminic acid, phosphate and thiol groups of pyruvate kinase isoenzymes from Morris hepatoma 7777 and normal rat liver

Amino-acid composition of pyruvate kinase M2 isoenzyme variants from rat liver and Morris hepatoma 7777

Kinetic properties of phosphofructokinase and pyruvate kinase in the midgut gland and abdominal muscle of the crayfish Orconectes limosus Raf. [Crustacea: Decapoda] after injections of 20-hydroxyecdysone

Pyruvate kinase - a key enzyme of glycolysis in the tissues of selected snails of Poland

Effect of high-protein diet on glycolytic processes in skeletal muscles of exercising rats