These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Evidence for formation of a rabbit liver aldolase--rabbit liver fructose-1,6-bisphosphatase complex.
    Author: MacGregor JS, Singh VN, Davoust S, Melloni E, Pontremoli S, Horecker BL.
    Journal: Proc Natl Acad Sci U S A; 1980 Jul; 77(7):3889-92. PubMed ID: 6253999.
    Abstract:
    The ability of rabbit liver aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphatate-lyase, EC 4.1.2.13) and rabbit liver fructose-1,6-bisphosphatase (Fru-P2ase; D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) to partition into the gel phase of Ultrogel AcA 34 is decreased in a mixture of the two enzymes. Titration experiments indicate that a 1:1 complex is formed. The value for the distribution coefficient of the complex corresponds to a molecular mass of 300,000 daltons, the value expected for a dimer containing one mole of each enzyme protein. Complex formation was not observed when either liver enzyme was replaced by the corresponding isozyme from rabbit muscle. The susceptibility of liver Fru-P2ase to limited proteolysis by subtilisin was reduced in the presence of liver aldolase, but not when the latter was replaced by muscle aldolase, suggesting that the conformation of Fru-P2ase is altered in the complex. Limited proteolysis of liver aldolase abolishes its ability both to form the heterodimer and to protect Fru-P2ase from modification by subtilisin.
    [Abstract] [Full Text] [Related] [New Search]