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- W2058484695 abstract "The mutants am1 and am3 each produce a defective variety of glutamate dehydrogenase. The am1 variety has no enzymic activity, while the am3 variety has abnormal activity distinguishable from that of wild-type enzyme. The two varieties are partially separable from each other by chromatography on DEAE-cellulose. Heterocaryons containing nuclei of both mutant types produce a mixture of enzyme types including am1 and am3-like components together with a chromatographically intermediate component (“complementation enzyme”) having properties approaching those of wild-type enzyme. Purified am1 and am3 proteins, isolated from separately grown mutants, can interact to form a mixture of enzyme types very similar to that found in the heterocaryon. The best conditions found for the interaction are adjustment of the mixture to pH 5·8, followed by re-adjustment to pH 7·4. When the concentration of one mutant protein is kept constant while that of the other is varied, the yield of complementation enzyme increases with concentration of the varying component up to a maximum beyond which the yield declines somewhat. The optimum ratio for a given amount of protein is 2 to 3 parts of the am1 variety to 1 part of am3. Although there is evidence which strongly indicates that the enzyme consists of a number of probably identical subunits, a preliminary ultracentrifuge analysis has not given any indication of dissociation of either mutant protein into subunits at pH 5·8 ; the S values for the two varieties were found to be rather similar to each other and to that of wild-type, and were no lower at pH 5·8 than at pH 7·4. The in vitro complementation reaction mixture appeared homogeneous in the ultracentrifuge and resembled the original proteins in sedimentation rate. It is considered that complementation enzyme is formed as a result of the exchange of polypeptide subunits between the interacting proteins." @default.
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- W2058484695 title "Complementation at the am locus of Neurospora crassa: a reaction between different mutant forms of glutamate dehydrogenase" @default.
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- W2058484695 doi "https://doi.org/10.1016/s0022-2836(63)80049-2" @default.
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