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

• Autorzy: Ignacak J. , Guminska M.
• Języki publikacji: EN

Abstrakty

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.

Słowa kluczowe

EN

affinity chromatography; pyruvate kinase; hepatoma; Blue Sepharose CL-6B; Morris hepatoma; liver; rat

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1993
• Tom: 40
• Numer: 2
• Opis fizyczny: p.261-267,fig.

Twórcy

autor

Ignacak J.

• Medical Academy, ul.Kopernika 7, 31-034 Krakow, Poland

autor

Guminska M.

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