Abstract
The apo/holo hydrid dimer of cytosolic aspartate aminotransferase from pig heart has been isolated by isoelectric focusing from a semi-reconstituted apo enzyme preparation. Comparison of the catalytic center activity and of the optical features of the coenzyme chromophore of the hybrid containing one active center with that of the homomer containing two revealed no differences in these properties and suggests that the subunits function independently from one another. However, differential thermal inactivation studies of hybrids and of homomers showed that the subunit carrying the coenzyme markedly stabilizes the structure of the neighboring subunit. Thus, coenzyme binding elicits functionally mute conformational changes which extend to and across the subunit interface.
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