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

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.

1968 ◽  
Vol 110 (2) ◽  
pp. 193-200 ◽  
Author(s):  
J. M. Gillespie ◽  
T. Haylett ◽  
H. Lindley

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.


1955 ◽  
Vol 8 (4) ◽  
pp. 537 ◽  
Author(s):  
DH Simmonds

The amino acid composition of 16-hr 6N HCI hydrolysates of three qualities of commercially classified wools has now been determined using the technique of Moore and Stein (1951). In this paper the results obtained on samples of Merino 70's and Corriedale 56's wool are compared with those previously reported for Merino wool of 64's quality. The overall pattern of the amino acid composition of the three wools is similar although small variations between the wools are observed with some of the amino acids.


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.


1979 ◽  
Vol 59 (2) ◽  
pp. 299-305 ◽  
Author(s):  
S. DUBETZ ◽  
E. E. GARDINER ◽  
D. FLYNN ◽  
A. IAN DE LA ROCHE

Grain from hard red spring wheat (Triticum aestivum ’Neepawa’) grown with nine rates of N fertilizer (0–400 kg/ha) was analyzed for total N, non-protein N (NPN), and amino acids. In addition, the amino acid compositions of the various soluble protein fractions were determined. The percentages of total N, NPN, and protein N of the grain increased with each 50-kg increment of N up to the 150-kg rate. The proportions of glutamate, proline, and phenylalanine in the seed increased whereas threonine, serine, glycine, alanine, and valine decreased with the first three or four increments of N fertilizer. With increasing N content in the seed, the proportions of albumin, globulin, and glutenin 2 decreased while the proportions of gliadin and glutenin 1 increased. The various protein fractions differed from each other in amino acid composition but the amino acid composition of each fraction was not influenced significantly by N application.


2010 ◽  
Vol 47 (6) ◽  
pp. 656-661 ◽  
Author(s):  
Moriyike Esther Ogunbusola ◽  
Tayo Nathaniel Fagbemi ◽  
Oluwatooyin Faramade Osundahunsi

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