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1

Rabbit muscle fructose-1,6-bisphosphatase is phosphorylated in vivo

100%
Rakus D., Zarzycki M., Dzugaj A.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr 1
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 Km and kcat 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.
2

Aldolase A is present in smooth muscle cell nuclei

84%
Mamczur P., Dzugaj A.
Acta Biochimica Polonica
|
2008
|
tom 55
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nr 4
799-805
Previously we have shown that aldolase (ALD; EC 4.1.2.13) is present in cardiomyocyte nuclei. Now, we focused our attention on ALD localization in smooth muscle cells. Immunocytochemical methods were used to study the subcellular localization of ALD. Aldolase was localized in the cytoplasm as well as in the nuclei. Within the nuclei ALD was located in the heterochromatin region. Native polyacrylamide gel electrophoresis followed by aldolase activity staining in gel was used to study the ALD isoenzyme pattern in porcine smooth muscle cells. Two ALD isoenzymes, A and C, were found in these cells but in the nuclei only the muscle isoenzyme was detected. To support the nuclear localization of ALD, measurement of aldolase activity in the smooth muscle cell nuclei isolated from porcine stomach was performed. The ALD activity in the isolated nuclei was detectable only after preincubation of the nuclear fraction with Triton X-100 and high concentration of KCl.
3

Seasonal changes in activity of some enzymes in the European bison Bison bonasus

84%
Gill J.
Acta Theriologica
|
1992
|
tom 37
|
nr 3
4

Changes in aldolase and glucose-6-phosphate isomerase activity in serum, liver and kidney of rabbits during starvation and immobilization

84%
Kolataj A., Lach H., Srebro Z., Sura P.
Acta Biologica Cracoviensia. Series Zoologia
|
2000
|
tom 42
5

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

84%
Saroop S., Chanda S. V., Singh Y. D.
Acta Physiologiae Plantarum
|
1996
|
tom 18
|
nr 4
6
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Some specific and non-specific phosphatases in the sporocyst of Fasciola hepatica. 3. Enzymes associated with glycolysis

84%
Humiczewska M.
Wiadomości Parazytologiczne
|
1997
|
tom 43
|
nr 4
Using histochemical and cytophotometric methods, enzymes associated with anaerobie glycolysis: glucose-6-phosphatase, hexokinase, and aldolase in the developing sporocysts of Fasciola hepatica were studied. Highest activity of these enzymes was found in the germ balls in the sporocysts, at all phases of their development, which is related to intensive proliferation and differentiation of the embryos developing inside the germ balls.
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