Malate dehydrogenase from thermophilic and mesophilic bacteria. Molecular size, subunit structure, amino acid composition, immunochemical homology, and catalytic activity

Biochemistry ◽  
1980 ◽  
Vol 19 (10) ◽  
pp. 2017-2022 ◽  
Author(s):  
T. K. Sundaram ◽  
I. P. Wright ◽  
A. E. Wilkinson
Keyword(s):  
Catalytic Activity ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Malate Dehydrogenase ◽  
Acid Composition ◽  
Molecular Size ◽  
Subunit Structure ◽  
Mesophilic Bacteria

scholarly journals Ribitol dehydrogenase from Klebsiella aerogenes. Purification and subunit structure

1974 ◽  
Vol 141 (3) ◽  
pp. 693-700 ◽  
Author(s):  
Susan S. Taylor ◽  
Peter W. J. Rigby ◽  
Brian S. Hartley
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Subunit Structure ◽  
Klebsiella Aerogenes ◽  
Peptide Maps ◽  
Ribitol Dehydrogenase

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.

Amino Acid Composition of Hemerythrin in Relation to Subunit Structure

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