scholarly journals Human adenine phosphoribosyltransferase. Affinity purification, subunit structure, amino acid composition, and peptide mapping.

1979 ◽  
Vol 254 (15) ◽  
pp. 6951-6955
Author(s):  
J A Holden ◽  
G S Meredith ◽  
W N Kelley
1974 ◽  
Vol 141 (3) ◽  
pp. 693-700 ◽  
Author(s):  
Susan S. Taylor ◽  
Peter W. J. Rigby ◽  
Brian S. Hartley

Ribitol dehydrogenase has been purified to homogeneity from several strains of Klebsiella aerogenes. One strain yields 3–6g of pure enzyme from 1kg of cells. The enzyme is a tetramer of four subunits, mol.wt. 27000. Preliminary studies of the activity of the enzyme are reported. Peptide ‘maps’ together with the amino acid composition indicate that the subunits are identical.


1971 ◽  
Vol 51 (1) ◽  
pp. 138-147 ◽  
Author(s):  
Howard Feit ◽  
Gary R. Dutton ◽  
Samuel H. Barondes ◽  
Michael L. Shelanski

The subunit protein of microtubules, tubulin, has been demonstrated to be present in isolated nerve endings by gel electrophoresis, amino acid composition, and peptide mapping. The tubulin constitutes approximately 28% of the soluble protein of the nerve endings. The transport of tubulin to the nerve endings has been demonstrated and its relationship to slow transport is discussed.


Science ◽  
1963 ◽  
Vol 141 (3576) ◽  
pp. 166-167 ◽  
Author(s):  
W. R. Groskopf ◽  
J. W. Holleman ◽  
I. M. Klotz ◽  
S. Keresztes-Nagy ◽  
E. Margoliash

Biochemistry ◽  
1972 ◽  
Vol 11 (14) ◽  
pp. 2699-2703 ◽  
Author(s):  
Donald J. W. Burns ◽  
Lewis L. Engel ◽  
John L. Bethune

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