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. 1966 Jan;98(1):210–214. doi: 10.1042/bj0980210

Formation of glucose from hexoses, pentoses, polyols and related substances in kidney cortex

H A Krebs 1, Patricia Lund 1
PMCID: PMC1264817  PMID: 5938645

Abstract

1. Slices of rat kidney cortex, on incubation in a saline medium, formed d-glucose from the following substances: d-fructose, d-galactose, d-mannose, l-sorbose, l-arabinose, d-xylose, glycerol, myo-inositol, l-iditol, sorbitol, xylitol, ribitol, methylglyoxal, dihydroxyacetone, l-glyceraldehyde, d-glyceraldehyde, dl-glyceraldehyde, dl-glycerate. Values for the rates of glucose formation from these precursors are given. 2. No glucose was formed from l-rhamnose, d-arabitol, d-arabinose, d-ribose, l-fucose, d-lyxose, mannitol, dulcitol, d-glucuronate, propane-1,2-diol and propan-2-ol. 3. The pathways of glucose formation from the various precursors are discussed (Scheme 1). 4. l-Glyceraldehyde inhibited the formation of glucose from d-glyceraldehyde.

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Selected References

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  1. ABRAHAM S., FITCH W. M., CHAIKOFF I. L. Mannose metabolism and the demonstration of mannokinase and phosphomannoisomerase activities in the lactating rat mammary gland. Arch Biochem Biophys. 1961 May;93:278–282. doi: 10.1016/0003-9861(61)90262-4. [DOI] [PubMed] [Google Scholar]
  2. ANDERSON L., COOTS R. H. Metabolism of 2-14C-myo-inositol in the rat. Biochim Biophys Acta. 1958 Jun;28(3):666–667. doi: 10.1016/0006-3002(58)90549-3. [DOI] [PubMed] [Google Scholar]
  3. BLAKLEY R. L. The metabolism and antiketogenic effects of sorbitol; sorbitol dehydrogenase. Biochem J. 1951 Aug;49(3):257–271. doi: 10.1042/bj0490257. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. BUBLITZ C., KENNEDY E. P. Synthesis of phosphatides in isolated mitochondria. III. The enzymatic phosphorylation of glycerol. J Biol Chem. 1954 Dec;211(2):951–961. [PubMed] [Google Scholar]
  5. BURNS J. J., TROUSOF N., EVANS C., PAPADOPOULOS N., AGRANOFF B. W. Conversion of myo-inositol to D-glucuronic acid and L-gulonic acid in the rat. Biochim Biophys Acta. 1959 May;33(1):215–219. doi: 10.1016/0006-3002(59)90516-5. [DOI] [PubMed] [Google Scholar]
  6. CHARALAMPOUS F. C. Biochemical studies on inositol. VI. Mechanism of cleavage of inositol to D-glucuronic acid. J Biol Chem. 1960 May;235:1286–1291. [PubMed] [Google Scholar]
  7. CORI G. T., OCHOA S., SLEIN M. W., CORI C. F. The metabolism of fructose in liver; isolation of fructose-I-phosphate and inorganic pyrophosphate. Biochim Biophys Acta. 1951 Jul;7(2):304–317. doi: 10.1016/0006-3002(51)90032-7. [DOI] [PubMed] [Google Scholar]
  8. Cori C. F., Shine W. M. THE FORMATION OF CARBOHYDRATE FROM GLYCEROPHOSPHATE IN THE LIVER OF THE RAT. Science. 1935 Aug 9;82(2119):134–135. doi: 10.1126/science.82.2119.134-a. [DOI] [PubMed] [Google Scholar]
  9. DIPIETRO D. L. SOME ASPECTS OF D-FRUCTOSE METABOLISM IN RAT LIVER. J Biol Chem. 1964 Dec;239:4051–4055. [PubMed] [Google Scholar]
  10. Exton J. H., Edson N. L. The antiketogenic action of sorbitol. Biochem J. 1964 Jun;91(3):478–483. doi: 10.1042/bj0910478. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. HOLLMANN S., TOUSTER O. The L-xylulose-xylitol enzyme and other polyol dehydrogenases of guinea pig liver mitochondria. J Biol Chem. 1957 Mar;225(1):87–102. [PubMed] [Google Scholar]
  12. HOLZER H., HOLLDORF A. Anreicherung, Charakterisierung und biologische Bedeutung einer D-Glycerat-kinase aus Rattenleber. Biochem Z. 1957;329(4):283–291. [PubMed] [Google Scholar]
  13. HUTCHESON R. M., REYNOLDS V. H., TOUSTER O. The reduction of L-xylulose to xylitol by guinea pig liver mitochondria. J Biol Chem. 1956 Aug;221(2):697–709. [PubMed] [Google Scholar]
  14. KALCKAR H. M. Uridinediphospho galactose; metabolism, enzymology, and biology. Adv Enzymol Relat Subj Biochem. 1958;20:111–134. doi: 10.1002/9780470122655.ch4. [DOI] [PubMed] [Google Scholar]
  15. KATTERMANN R., DOLD U., HOLZER H. [D-Glycerate in fructose degradation in the liver]. Biochem Z. 1961;334:218–226. [PubMed] [Google Scholar]
  16. KREBS H. A., BENNETT D. A., DE GASQUET P., GASQUET P., GASCOYNE T., YOSHIDA T. Renal gluconeogenesis. The effect of diet on the gluconeogenic capacity of rat-kidney-cortex slices. Biochem J. 1963 Jan;86:22–27. doi: 10.1042/bj0860022. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. KREBS H. A., YOSHIDA T. RENAL GLUCONEOGENESIS. 2. THE GLUCONEOGENIC CAPACITY OF THE KIDNEY CORTEX OF VARIOUS SPECIES. Biochem J. 1963 Nov;89:398–400. doi: 10.1042/bj0890398. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. KREBS H. THE CROONIAN LECTURE, 1963. GLUCONEOGENESIS. Proc R Soc Lond B Biol Sci. 1964 Mar 17;159:545–564. doi: 10.1098/rspb.1964.0019. [DOI] [PubMed] [Google Scholar]
  19. LANDAU B. R., MERLEVEDE W. Initial reactions in the metabolism of D- and L-glyceraldehyde by rat liver. J Biol Chem. 1963 Mar;238:861–867. [PubMed] [Google Scholar]
  20. LARDY H. A., WIEBELHAUS V. D., MANN K. M. The mechanism by which glyceraldehyde inhibits glycolysis. J Biol Chem. 1950 Nov;187(1):325–337. [PubMed] [Google Scholar]
  21. MENDELOFF A. I., WEICHSELBAUM T. E. Role of the human liver in the assimilation of intravenously administered fructose. Metabolism. 1953 Sep;2(5):450–458. [PubMed] [Google Scholar]
  22. McCORKINDALE J., EDSON N. L. Polyol dehydrogenases. I. The specificity of rat-liver polyol dehydrogenase. Biochem J. 1954 Jul;57(3):518–523. doi: 10.1042/bj0570518. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. SHULL K. H., MILLER O. N. Formation in vivo of glycogen by certain intermediates of the lactate-propanediol pathway. J Biol Chem. 1960 Mar;235:551–553. [PubMed] [Google Scholar]
  24. SMITH M. G. Polyol dehydrogenases. 4. Crystallization of the L-iditol dehydrogenase of sheep liver. Biochem J. 1962 Apr;83:135–144. doi: 10.1042/bj0830135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. TOUSTER O., SHAW D. R. Biochemistry of the acyclic polyols. Physiol Rev. 1962 Apr;42:181–225. doi: 10.1152/physrev.1962.42.2.181. [DOI] [PubMed] [Google Scholar]
  26. TUNG T. C., LING K. H., BYRNE W. L., LARDY H. A. Substrate specificity of muscle aldolase. Biochim Biophys Acta. 1954 Aug;14(4):488–494. doi: 10.1016/0006-3002(54)90228-0. [DOI] [PubMed] [Google Scholar]
  27. WIELAND O., SUYTER M. Glycerokinase; Isolierung und Eigenschaften des Enzyms. Biochem Z. 1957;329(4):320–331. [PubMed] [Google Scholar]

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