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J. Biochem, 1978, Vol. 83, No. 3 821-825
© 1978 Japanese Biochemical Society

research-article

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

Nanaya TAMAKI*, Keiko KIMURA* and Takao HAMA**

*Laboratory of Nutritional Chemistry, Faculty of Nutrition Kobe-Gakuin University Tarumi-ku, Kobe, Hyogo 673
**Laboratory of Physiological Chemistry, Faculty of Pharmacy, Kobe-Gakuin University Tarumi-ku, Kobe, Hyogo 673

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.


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