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YILMAZ, Seval
Turkish journal of veterinary & animal sciences, 2003, Volume: 27, Issue: 4Journal Article
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. 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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