Studies on the Oligomeric Structure of Yeast Aldehyde Dehydrogenase by Cross-Linking with Bifunctional Reagents

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Abstract
The molecular weight of yeast aldehyde dehydrogenase determined by sucrose density gradient centrifugation was 207,000±13, 000. The enzyme activity was proportional to the enzyme concentration in the range of 2×10−11 M to 1×10−7 M. Cross-linking patterns obtained with yeast aldehyde dehydrogenase after treatment with a series of diimidoesters of increasing chain lengths with different reaction times resulted in the appearance of tetramers as the largest cross-linked product of the enzyme subunits. The molecular weights of its monomer, dimer, trimer, and tetramer were, 57,000, 114,000, 171,000, and 228,000, respectively, as estimated from their mobilities on SDS-electrophoresis. In tetramers monomers are probably assembled in a heterologous square arrangement.