Self-association of lyophilized horse liver alcohol dehydrogenase. |
| |
| Authors: | J B Ross E L Chang D C Teller |
| |
| Affiliation: | Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218, USA;Department of Chemistry, University of Washington, Seattle, Washington 98195, USA;Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA |
| |
| Abstract: | The molecular weights of lyophilized and non-lyophilized horse liver alcohol dehydrogenase have been compared by quasi-elastic light scattering, and ultracentrifugation. Whereas the non-lyophilized enzyme has the expected molecular weight of 78 000, the lyophilized enz)me has an initial molecular weight of about 10(6) which increases with time by an endothermic process. This result shows that any physical measurement using lyophilized liver alcohol dehydrogenase to investigate the enzyme mechanism, which relies upon the molecular size, will be invalid. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
