Molecular characterization of tumor associated glyceraldehyde-3-phosphate dehydrogenase.

Here we describe the purification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from normal leukocytes of healthy subjects and leukocytes of chronic myeloid leukemia (CML) patients and from normal mouse muscle and sarcoma tissue. The data indicate that some properties of GAPDH of leukocytes of CML patients and sarcoma tissues are similar and also similar to those of EAC (Ehrlich ascites carcinoma) cellular GAPDH but distinctly different from those of the normal cellular GAPDH. Polyclonal antiserum raised against the 54 kDa subunit of EAC cell GAPDH strongly reacted with GAPDH of leukocytes of CML patients and sarcoma tissue GAPDH only and weakly reacted with GAPDH of normal leukocyte and normal muscle and a variety of other tissues of normal rats. Both the subunits of GAPDH of sarcoma tissues were partially sequenced from the N-terminus and compared with the known sequences of GAPDH. The altered properties of GAPDH of three different malignant sources might be common feature of all malignant cells, which is discussed in relation to glycolysis and malignant aberrations.