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Phosphofructokinase isozymes of Morris hepatomas

1981; Elsevier BV; Volume: 212; Issue: 1 Linguagem: Inglês

10.1016/0003-9861(81)90337-4

1096-0384

George Dunaway, Durdana Naqui, Dale Kruep, James Thrasher, Harold P. Morris,

Lipid metabolism and biosynthesis

Abstract In this paper we demonstrate by DEAE-cellulose column chromatography, agarose gel electrophoresis, and immunological techniques that at least three phosphofructokinase (PFK) isozymes exist in Morris hepatomas regardless of their state of differentiation. The major PFK isozyme in Morris hepatomas was found to be the major liver PFK isozyme (PFK-L 2 ) which varied from approximately 4.7 units/g in poorly differentiated hepatomas to approximately 2.5 units/g in liver, as well as highly and well-differentiated hepatomas. One of the minor isozymes, the hepatoma type PFK (PFK-H), was not present in liver and was found by resolution of DEAE-cellulose chromatography and immunological studies to be greater in the poorly differentiated hepatomas (approximately 30%) compared to the well and highly differentiated hepatomas (5–10%). Further, immunological studies indicated that in the poorly differentiated hepatomas 25–30% of the total PFK activity could be precipitated by both PFK-L 2 and muscle type PFK (PFK-M) antisera. In order to examine this observation more closely, supernates from the poorly differentiated hepatoma 3924A were incubated with each type of antiserum. As shown by agarose gel electrophoresis, incubation with PFK-L 2 antiserum resulted in the loss of PFK-L 2 and PFK-H isozymes, whereas incubation with PFK-M antiserum resulted in the loss of PFK-H, and the other minor hepatoma PFK isozyme. These data indicate that PFK-M is one of the minor hepatoma isozymes and that the other, PFK-H, has common antigenic determinants with PFK-M and PFK-L 2 .