Hybridization of variants of an oligomeric protein can provide information about the number of subunits in the oligomer. Such hybridization studies have generally been done in vitro using either genetic variants or chemically modified enzyme. A disadvantage of in vitro hybridization is that it can only be applied to proteins which can be reversibly dissociated into subunits. This paper presents two methods of obtaining electrophoretic variants of bacterial enzymes. The variants are hybridized in vivo, by random association of newly synthesized subunits. This method is not restricted to proteins which are reversibly dissociable and avoids artifacts which can arise in the course of chemical modification of protein. The variant protein used is enzymatically active and thus is likely to be similar to wild-type protein. The method has been applied to two enzymes, histidinol dehydrogenase and 6-phosphogluconate dehydrogenase. Each of these enzymes seems to be composed of two subunits.
|Original language||English (US)|
|Number of pages||4|
|State||Published - 1971|
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