scholarly journals Comparison of calregulins from vertebrate livers

1987 ◽  
Vol 242 (1) ◽  
pp. 245-251 ◽  
Author(s):  
N C Khanna ◽  
M Tokuda ◽  
D M Waisman
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Fluorescent Probe ◽  
Structural Properties ◽  
Acid Composition ◽  
Protein Fluorescence ◽  
Binding Properties ◽  
Induced Changes ◽  
Intrinsic Protein Fluorescence ◽  
Peptide Maps

Calregulins were purified from bovine, rabbit and chicken liver, and their structural properties were compared. Significant differences between the three calregulins include a lower Mr for chicken calregulin (57,000) than for rabbit and bovine calregulin (63,000), and the glycosylation of only bovine calregulin. Amino acid composition and peptide maps of the three calregulins were very similar. No major differences were detected in the Ca2+-binding properties of the three proteins. Zn2+-induced changes in calregulin conformation and hydrophobicity monitored by intrinsic protein fluorescence and the hydrophobic fluorescent probe 8-anilino-1-naphthalenesulphonate were very similar, suggesting that the Zn2+-dependent increase in the hydrophobicity of bovine, rabbit and chicken calregulin was conserved. These studies more fully define what is a calregulin, demonstrate that calregulin is a relatively invariant constituent of vertebrate liver, and indicate that calregulin structure has been highly conserved in bovine, chicken and rabbit liver.

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.

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.

scholarly journals Studies on Reduced Wool V. A Comparison of the Two Major Components

1965 ◽  
Vol 18 (6) ◽  
pp. 1207 ◽  
Author(s):  
EOP Thompson ◽  
IJ O'donnell
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Deae Cellulose ◽  
Major Protein ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Protein Components ◽  
Wool Proteins ◽  
Peptide Maps

Starch-gel electrophoresis of wool proteins extracted from reduced and carboxymethylated wool gives a complex pattern in which there are two major protein bands. By a combination of chromatography on DEAE-cellulose and gelfiltration in buffers containing 8M urea these two protein components have been isolated. The amino acid composition and some properties of these two fractions are reported. A comparison of the amino acid composition and of peptide maps of tryptic digests of the two fractions shows distinct differences between them, and by labelling with 2-[14C]iodoacetate the distribution of the peptides containing S-carboxymethylcysteine residues were also shown to be different.

Sign in / Sign up

Export Citation Format

Share Document