Normal ve diabetik rat karaciğer dokusunda prüvat kinazın bazı kinetik özelliklerinin karşılaştırılması

Wistar-Albino cinsi erkek ratlara tek doz streptozocin (60 mg/kg) intraperitoneal verilerek diabetes mellitus oluşturulmuştur. Normal ve streptozosin etkisi ile diabet oluşturulan rat karaciğer dokusunda pirüvat kinaz enziminin kinetik özellikleri araştırılmıştır. Normal rat karaciğer doku pirüvat kirazının inkübasyon zamanı 15 dakika, optimum pH'sı 8; diabetik rat karaciğer doku pirüvat kinazmın inkübasyon zamanı 10 dakika, optimum pH'sı 7 olarak bulunmuştur. Magnezyum klorür ve potasyum klorür, normal ve diabetik rat karaciğer dokusunu aktive etmiştir. Enzim substrat olan fosfoenolpirüvat fruktoz l ,6 difosfat yokluğunda sigmoidal eğri gösterirken, fruktoz 1,6 difosfat varlığında eğri hiperbolik Michaelis-Menten kinetiğine dönüşmektedir. Pirüvat kinazmın fosfoenolpirüvat için Km değerinin normal ve diabetik karaciğer dokusunda farklılıklar gösterdiği ve fruktoz 1,6 difosfatın Km değerini düşürdüğü tespit edilmiş olup diabetik karaciğer dokusunda enzimin fosfoenolpirüvata ilgisinin azaldığı saptanmıştır.

Comparison of some kinetic properties of pyruvati kinase in liver tissue of normal and diabetic rats

Diabetes mellitus was induced in Wistar-Albino type male rats with a single dose of streptozotocin (60 mg/kg intraperitoneally). The kinetic properties of pyruvate kinase were investigated in normal and diabetic rat liver tissue. In normal rat liver tissue, the incubation period of pyruvate kinase was 15 min and the optimum pH was 8. In diabetic rat liver tissue, the incubation period of pyruvate kinase was 10 min and the optimum pH was 7. Activation was found in normal and diabetic rat liver tissues with magnesium chloride and potassium chloride. Phospho(enol)pyruvate is an enzyme substrate; in the absence of the fructose-1,6-diphosphate its graphic showed a sigmoidal plot, and in the presence of the fructose-1,6-diphosphate its graphic turned into a hyperbolic plot of Michaelis-Menten kinetics. Different Km pyruvate kinase values for phospho(enol)pyruvate were found in normal and diabetic liver tissues, and the Km value of fructose-1,6-diphosphate was determined as low. A low phospho(enol)pyruvate enzyme affinity was identified in diabetic liver tissue.

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  • Altuntaş, Y.: Diabetes Mellitus'un Tanımı, Tanısı ve Sınıflaması. Ed. Yenigün M. Her Yönüyle Diabetes Mellitus. Nobel Tıp Kitapevi. 51-67:2001.
  • Pilkis, S.J., EI-Maghrabi, M.R., Clauss, ' T.H.: Hormonal Regulation of Hepatic Gluconeogenesis and Glycolysis. Annu. Rev. Biochem. 1988; 57: 755-783.
  • Sochor, ML, Kunjara, S., Baquer, N.Z., Mclean, P.: Regulation of Glucose Metabolism in Livers and Kidneys of NOD Mice. Diabetes. 1991:40:1467-1471.
  • Kaloyianni-Dimitriades, M.G., Beis, I.D.: Purification, Catalytic and Regulatory Properties of Rana ridibunda Erythrocyte Pyruvate Kinase. Comp. Biochem. Phyciol. 1984; 7B: 245-250.
  • Muirhead, H.: Isoenzymes of Pyruvate Kinase. Biochem. Soc. Trans. 1990; 18: 193-196.
  • Imamura, K., Taniuchi, K., Tanaka, T.: Multimolecular Forms of Pyruvate Kinase. J. Biochem. 1972; 72: 1001-1015.
  • Imamura, K., Taniuchi, K., Tanaka, T.: Multimolecular Forms of Pyruvate Kinase from Rat and Other Mammalian Tissues. J.. Biochem. 1972; 71: 1043-1051.
  • Kiffmeyer, W.R., Farrar, W.W.: Purification and Properties of Pig Heart Pyruvate Kinase. J Protein Chem. 1991; 10: 585-591.
  • Reinacher, M., Eigenbrodt, E., Gerbracht, U., Zenk, G., Timmermann-Trosiener, I., Bentley, P., Waechter, F., Schulte- Hermann, R.: Pyruvate Kinase Isoenzymes in Altered Foci and Carcinoma of Rat Liver. Carcinogenesis. 1986; 7: 1351-1357.
  • Oskam, R., Van Els, C.A., Rijksem, G., Staal, G.E.: Pyruvate Kinase Isoenzymes and Differentiation of (Neuro-) Ectodermal Tumours. Tumour Biol. 1985; 6: 75-87.
  • Yılmaz, S., Üstündağ, B.: Streptozotosin ile Diabet Oluşturulan Ratların Karaciğer ve Böbrek Dokularında Pirüvat Kinaz Aktivite Düzeyleri. Turk. J. Vet. Anim. Sci. 2002; 26: 549-553.
  • Valera, A., Rodriguez-Gil, J.E., Bosch, F.: Vanadate Treatment Restores the Expression of Genes for Key Enzymes in the Glucose and Ketone Bodies Metabolism in the Liver of Diabetic Rats. J. Clin. Invest. 1993; 92: 4-11.
  • Beutler, E., Blume, K.G., Kaplan, J.C., Löhr, G.W., Ramot, B., Valentine, W.N.: International Committee for Standardization in Haematology: Recommended Methods for Red-Cell Enzyme Analysis. Br. J. Haematol. 1977; 35: 311 -340.
  • Saxena, A.K., Srivastava, P., Baquer, N.Z.: Effects of Vanadate on Glycolytic Enzymes and Malic Enzyme in Insulin-Dependent and - Independent Tissues of Diabetic Rats. Eur. J. Pharmacol. 1992; 1: 123-126.
  • Verhagen, J.N., Heijden, M.C.M., Dijken, J.J., Rijken, G., Kinderen, P.J., Unnik, J.A.M., Staal G.E.J.: Pyruvate Kinase in Normal Human Thyroid Tissue and Thyroid Neoplasms. Cancer. 1985; 55: 142-148.
  • Helmy, E., Unnik, A.M., Rijksen, G., Smits, G., Staal, J.: Cellular Expression of K-type Pyruvate Kinase in Normal and Neoplastic Human Tissues. Cancer. 1991; 68: 2595-2601.
  • Ignacak, J., Guminska, ML: Comparasion of Pyruvate Kinase Variants from Rat Liver and Morris Hepatoma 7777, Obtained by an Affinity Chromatography on Blue Sepharose CL-6B., Acta Biochim. Pol. 1993; 40: 261-267.
  • Cardenas, J.M., Dyson, R.D., Strandholm, J.J.: Bovine Pyruvate Kinases. I. Purification and Characterization of the Skeletal Muscle Isozyme. J. Biol. Chem. 1973; 248: 6931-6937.
  • Baranowska, B., Baranowski, T.: Pyruvate Kinase from Human Skeletal Muscle. Mol. Cell. Biochem. 1975; 6: 197-201..
  • Yılmaz, S.: İnsan Eritrosit ve Karaciğer Doku Pirüvat Kinazının Kinetik Özellikleri, Doktora Tezi. Sağlık Bilimleri Enstitüsü, Elazığ, 1997.
  • Leon, 0., Moran, A., Gonzalez, R: Purification and Characterization of Pyruvate Kinase from Muscle of the Sea Mollusc. Concholepas. Com. Biochem. Physiol., 1982; 72B: 65- 69.
  • Macfarlane, N., Ainsworth, S.: A Kinetic Study of Pig Pyruvate Kinase Activated by Fructose Diphosphate. Biochem. J. 1974; 139:499-508.
  • Balinsky, D., Cayanis, E., Bersohn, I.: Comparative Kinetic Study of Human Pyruvate Kinases Isolated from Adult and Foetal Livers and from Hepatoma. Biochemistry. 1973; 12: 863-870.
  • Berglund, L, Humble, E.: Kinetic Properties of Pig Pyruvate Kinases Type A from Kidney and Type M from Muscle. Arch. Biochem. Biophys. 1979; 195: 347-361.
  • Becker, K.J., Geyer H., Eigenbrodt, E., Schoner, W.: Purification of Pyruvate Kinase Isoenzymes Type Mt and M2 from Dog (Canis Familiaris) and Comparison of Their Properties with Those from Chicken and Rat. Comp. Biochem. Physiol. 1986; 83: 823-829.
  • Carbonell, J., Feliu, J.E., Marco, R., Sols, A.: Pyruvate Kinase. Classes of Regulatory Isoenzymes in Mammalian Tissues. Eur. J. Biochem. 1973; 37: 148-156.
  • Feliu, J.E., Diaz-Gil, J., Garcia-Canero, R., Gonsalvez, M.: Interconvertible Forms of Class A Pyruvate Kinase from Ehrlich Ascites Tumour Cells. FEBS Lett. 1975; 50: 334-338.
  • Balinsky, D., Cayanis, E., Bresohn, L: Enzymes of Carbohydrate Metabolism in Rat Hepatoma Induced by 3'-Methyl-4- Dimethylaminoazobenzene. Biochemistry. 1972; 12: 863-870.
  • Kedryna T., Guminska M., Marchut E.: Pyruvate Kinase from Cytosolic Fractions of the Ehrlich Ascites Tumour, Normal Mouse Liver and Skeletal Muscle. Biochim. Biophys. Acta. 1990; 1039: 130-133.
Turkish Journal of Veterinary and Animal Sciences-Cover
  • ISSN: 1300-0128
  • Yayın Aralığı: Yılda 6 Sayı
  • Yayıncı: TÜBİTAK
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