In Vitro Formation of Enzymatically Active Hybrid Proteins from E. Coli Alkaline Phosphatase CRM's
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Excerpt
In the model proposed by Brenner (1959) and Fincham (1960) to explain intra-cistronic (interallelic) complementation, monomer subunits derived from each of the mutated cistrons in the heterozygote interact in the same cytoplasm to form an active protein. This mechanism is based on the concept that proteins which can complement contain identical subunits and that mutationally altered monomers may sometimes form enzymatically active molecular hybrids. In the individual mutants these altered subunits are unable to produce active enzyme although they might form antigenically related protein (CRM).
Intra-cistronic complementation has recently been found to occur in vivo between several alkaline phosphatase negative (P−) mutants of E. coli (Garen and Garen, 1963), and chemical studies have shown that this enzyme is composed of two identical subunits (Rothman and Byrne, 1963). It was previously demonstrated that hybrid proteins could be obtained between enzymatically active forms of E. coli alkaline phosphatases (Levinthal, Signer, and Fetherolf,...
