Subunit dissociation and recombination of catalase isozymes.

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Abstract
Analysis by starch gel electrophoresis shows that there are 3 electrophoretic variants of catalase in maize endosperm. These variations are under genetic control. In the heterozygotes, catalase is resolved into 5 isozymes, 3 of which are hybrid enzymes with mobilities intermediate between the parental enzymes. These hybrid enzymes are formed by random combination of 2 types of monomers into tetramers. That catalase exists functionally as a tetramer is supported by experiments where mixtures of the 2 variants were frozen in 1[image] Nacl and were dissociated into monomers. On thawing, reassoclatlon into functional tetramers occurs. It is suggested that the monomer is the primary gene product and that the enzymatlcally active unit is an aggregate of these monomers into the tetramers. The results lend support to the subunit structure hypothesis of maize catalases.