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

scholarly journals Studies on Oxidized Wool V. Comparison of Protein Fractions Extracted From Wool by Peptide Mapping of Enzymic Digests

1962 ◽  
Vol 15 (3) ◽  
pp. 552 ◽  
Author(s):  
EOP Thompson ◽  
IJ O'donnell
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Peptide Mapping ◽  
Protein Fractions ◽  
Two Dimensional ◽  
Merino Wool ◽  
Peptide Maps

Peptide maps, which were prepared by two-dimensional ionophoresis of various enzymic digests of chromatographically resolvable fractions of a-keratose from Merino wool, have failed to reveal any readily detectable differences despite significant differences in amino acid composition. It is postulated that some contaminant protein which remains bound to the low-sulphur "mother" protein is responsible, in part, for the chromatographic heterogeneity and variation in amino acid composition of separated fractions. Peptide maps of a-keratoses derived from Lincoln and Merino wools are very similar.

scholarly journals Evidence of homology in a high-sulphur protein fraction (SCMK-B2) of wool and hair α-keratins

1968 ◽  
Vol 110 (2) ◽  
pp. 193-200 ◽  
Author(s):  
J. M. Gillespie ◽  
T. Haylett ◽  
H. Lindley
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Protein Fraction ◽  
Protein Component ◽  
Terminal Sequence ◽  
Merino Wool ◽  
Peptide Maps ◽  
Similar Peptide

Fractions corresponding to the S-carboxymethylated high-sulphur protein component SCMK–B2 isolated by Gillespie (1963) from Merino wool were prepared from five different wool samples and also from bovine hair. The six fractions showed great similarities in amino acid composition, and also gave very similar peptide ‘maps’ after tryptic and chymotryptic digestion. Some of the peptides were isolated from the different samples, and evidence is given that suggests that a sequence of at least 21 amino acids is common to all the fraction SCMK–B2 preparations. Further, all the fractions derived from the wool samples have the same acetylated heptapeptide for the N-terminal sequence, but one extra residue may be present in this N-terminal sequence in the protein from bovine hair. The general significance of these findings is discussed.

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