Modification of pyruvate kinase from the foot muscle of Patella caerulea (L) during anaerobiosis

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Abstract
Pyruvate kinase (PK) from the foot muscle of Patella carulea (L) is present as two variants. These variants are eluted by ion‐exchange chromatography from DEAE‐cellulose as peak I and peak II at different concentrations of KCl. Studies of their kinetic properties show that both variants of PK exhibit sigmoidal curves with respect to phosphoenolpyuvate (PEP), but the PK in peak I is more sensitive to the activation by PEP and fructose diphosphate (FDP) and less sensitive to inhibition by alanine, ATP, and H+ than the PK in peak II. The proportion of the two PK variants changes during anaerobiosis. The ratio of the number of units of enzyme in peak I to that in peak II increases up to the second hour and then decreases up to the eight hour of anaerobiosis. Studies on the electrophoretic mobility of these two variants on strips of cellulose acetate show that the less active from or peak II PK migrates more quickly toward the anode (Rf = 0.13) than the more active from or peak I PK (Rf = 0.07). Peak II PK, after treatment with alkaline phosphatase, exhibits kinetic properties and electrophoretic mobility quite similar to those of peak I PK. The above data suggest that the two variants of PK from the foot muscle of P. caerulea are interconvertible and the direction of the interconversion depends on the duration of anaerobiosis.

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