HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kashiwagura, T. Articles by Wilson, D. F. Search for Related Content PubMed PubMed Citation Articles by Kashiwagura, T. Articles by Wilson, D. F. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 259, Issue 1, 237-243, Jan, 1984

Dependence of gluconeogenesis, urea synthesis, and energy metabolism of hepatocytes on intracellular pH

T Kashiwagura, CJ Deutsch, J Taylor, M Erecinska and DF Wilson

The relationship of intracellular pH to extracellular pH has been measured in suspensions of isolated hepatocytes at 25 degrees C. The internal pH was found to be a linear function of external pH and it changed by 0.45 pH unit per 1.0 unit change in external pH. The internal [H+] was equal to the external [H+] at approximately pH 7.1. Gluconeogenesis, urea synthesis, and oxidative phosphorylation showed different dependencies on the intracellular pH. Gluconeogenesis was the most sensitive to changes in [H+] and it declined by 80% when the intracellular pH decreased from 7.1 to 6.9. Urea synthesis was less pH- dependent, decreasing by about 30% for the same change in the intracellular [H+] whereas respiratory rate showed very little dependence on pH at this temperature. Intracellular [ATP]/[ADP] decreased linearly from 8.5 to 1.5 as the intracellular pH increased from 6.8 to 7.6, while intracellular [Pi] was essentially constant at 3.2 nmol/mg of cells, wet weight. Cytochrome c became more reduced with increasing intracellular pH, from less than 10% at pH 6.8 to 35% at pH 7.7. The calculated free energy of hydrolysis of ATP was nearly independent of pH as was the free energy of electron transfer from the intramitochondrial NAD couple (calculated from the [acetoacetate]/[3-OH- butyrate] ratio) to cytochrome c.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				P. Sasi, S. P. Burns, C. Waruiru, M. English, C. L. Hobson, C. G. King, M. Mosobo, J. S. Beech, R. A. Iles, B. J. Boucher, et al. Metabolic Acidosis and Other Determinants of Hemoglobin-Oxygen Dissociation in Severe Childhood Plasmodium falciparum Malaria Am J Trop Med Hyg, August 1, 2007; 77(2): 256 - 260. [Abstract] [Full Text] [PDF]

				R. E. Shangraw and F. Jahoor Effect of liver disease and transplantation on urea synthesis in humans: relationship to acid-base status Am J Physiol Gastrointest Liver Physiol, May 1, 1999; 276(5): G1145 - G1152. [Abstract] [Full Text] [PDF]