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Science 28 August 1964:
Vol. 145. no. 3635, pp. 930 - 932
DOI: 10.1126/science.145.3635.930
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Articles

Electron Microscopic and Biochemical Studies of Pyruvate Dehydrogenase Complex of Escherichia coli

Humberto Fernandez-Moran 1, Lester J. Reed 2, Masahiko Koike 2, and Charles R. Willms 2

1 Department of Biophysics, University of Chicago, Chicago, Illinois
2 Clayton Foundation, Biochemical Institute, and Department of Chemistry, University of Texas, Austin

Examination with the electron microscope of the pyruvate dehydrogenase complex and its component enzymes from Escherichia coli indicates that the complex has a polyhedral structure with a diameter of about 300 to 350 angstroms and a height of 200 to 250 angstroms. The reconstituted complex closely resembles the native complex in appearance. A tentative model of this multienzyme complex is proposed on the basis of the correlated biochemical and electron-microscopic data


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Translational Control of Gene Expression.
A. L. Cline and R. M. Bock (1966)
Cold Spring Harb Symp Quant Biol 31, 321-333
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Electron Microscopic and Biochemical Characterization of Fraction I Protein.
R. Haselkorn, H. Fernandez-Moran, F. J. Kieras, and E. F. J. van Bruggen (1965)
Science 150, 1598-1601
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