PMID: 107973Jan 1, 1979

Modifications of aldolase during in vivo aging of rabbit red cells

F MennecierJ C Dreyfus


Crude hemolysates, partially purified aldolase and aldolase purified to homogeneity from reticulocytes and mature erythrocytes, were incubated with a specific antiserum raised against crystalline rabbit muscle aldolase. We show that the same aldolasic activity corresponds to a greater amount of antigen in older than in younger cells, in crude hemolysates as well as in the above mentioned preparations; that is to say, old-cell aldolase contains cross-reacting material (CRM). Properties of purified enzyme from reticulocytes and mature erythrocytes were compared to those of muscle crystalline aldolase: -- the molecular specific activity of purified aldolase from erythrocytes is lower than with crystalline muscle aldolase, i.e. CRM is maintained throughout the purification steps. -- the specific activity of red cell aldolase towards both substrates (FDP and F1P) is lower than that of crystalline muscle aldolase. However, the ratio of activity towards the two substrates FDP/F1P is decreased in erythrocytes and reticulocytes. -- no other difference was found: Michaelis constant towards FDP, thermodenaturation constant and C terminal extremities are identical as are the molecular weights.


Jun 28, 1977·Biochemistry·E Strapazon, T L Steck
Oct 17, 1974·Biochimica Et Biophysica Acta·F Mennecier, J C Dreyfus
Jul 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·C F Midelfort, A H Mehler
Sep 19, 1970·Nature·H Gershon, D Gershon


Jan 1, 1983·The International Journal of Biochemistry·A BartkowiakG Bartosz
Jan 1, 1980·Mechanisms of Ageing and Development·R B Burrows, P F Davison
Jan 1, 1980·Mechanisms of Ageing and Development·G Bartosz
Nov 1, 1981·Mechanisms of Ageing and Development·G BartoszW Retelewska

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