Rabbit muscle glyceraldehyle-3-phosphate dehydrogenase (GAPD) was dissociated into a subunit species via lauryl sulfate (LS). The incubation mixture prepared from active GAPD 10-5 M and LS 10-3 M showed a rapid loss of initial activity. Within 30 minutes after the addition of the powdered LS, there was a 50 percent loss in initial enzymatic activity. The appearance of the subunit species was verified by Sephadex (a crossed-linked dextran) molecular sieve studies. Using a column buffer containing 0.01 M acetic acid, 0.10 M NaCl and 0.005 M LS at 25° C., with a pH of 6.1 ± 0.1, elution patterns of GAPD, conalbumin, hemoglobin and lysozyme were used to calibrate a G-100 Sephadex column. From the Sephadex gel filtration studies, it was discerned that GAPD in the presence of LS acts as a dimer.
Proceedings of the Iowa Academy of Science
© Copyright 1968 by the Iowa Academy of Science, Inc.
Marti, G. E. and White, B. J.
"Dissociation of Glyceraldehyde-3-Phosphate Dehydrogenase with Sodium Dodecyl Sulfate,"
Proceedings of the Iowa Academy of Science: Vol. 75:
, Article 18.
Available at: https://scholarworks.uni.edu/pias/vol75/iss1/18