Abstract
THE heterogeneous population of rat liver1 has led to a discussion of the interpretation of enzyme activities based on whole liver or whole liver proteins2. Recent interest in the properties of suspensions of parenchymatous liver cells3,4 has raised the possibility of using such cells as reference base for enzyme determinations. By shaking rat liver slices in calcium-free citrated Krebs-Ringer phosphate buffer with added glucose, passing the slices through graded sieves to break them into the component cells, centrifuging and resuspending the sediment, we have shown5,6 that the cells of such suspensions leak most of their content of glutamic pyruvic transaminase while retaining glutamic oxalacetic transaminase. Subsequent studies have shown that in general between 70 and 90 per cent of lactic acid dehydrogenase, ‘TPN-linked’ isocitric dehydrogenase and glucose-6-phosphate dehydrogenase are similarly lost from the cells in the course of making the preparation. The leakage of lactic acid dehydrogenase was not prevented by making the medium between 0.01 M and 1 M in pyruvate both with and without the addition of 2–5 per cent bovine albumen fraction V, by the presence of adenosine triphosphate (750 mgm. per cent) crystalline human oxyhæmoglobin (5–10 per cent) and carbonic anhydrase, the latter two being used both singly and in combination. By making the medium 20 per cent in washed human red blood cells the leakage appeared to be inhibited7.
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References
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HENLEY, K., SORENSEN, O. & POLLARD, H. Some Enzymatic Properties of Suspensions of Parenchymatous Liver Cells. Nature 184, 1400 (1959). https://doi.org/10.1038/1841400a0
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DOI: https://doi.org/10.1038/1841400a0
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