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 The Amino Acid Composition of Keratins

1955 ◽  
Vol 8 (4) ◽  
pp. 537 ◽  
Author(s):  
DH Simmonds
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Merino Wool

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.

scholarly journals The Macroheterogeneity of Type I Tyrosine-rich Proteins of Merino Wool

1974 ◽  
Vol 27 (6) ◽  
pp. 617 ◽  
Author(s):  
J M Gillespie ◽  
MJ Frenkel
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Quaternary Ammonium ◽  
Deae Cellulose ◽  
Type I ◽  
Merino Wool ◽  
Poor Family ◽  
Tyrosine Content

The cystine-poor family of tyrosine-rich proteins of wool as their S-carboxymethyl derivatives has been shown by chromatography on quaternary ammonium ethylcellulose (QAE-cellulose) at pH 10� 5 to consist of 10 groups of proteins which span a threefold range of tyrosine content and vary in many other amino acids, particularly S-carboxymethylcysteine. Electrophoresis at pH 8�9 revealed that most fractions contain two or more components and by further chromatography of five of these groups at pH 8�3 on DEAE-cellulose 10 components have been isolated. The amino acid composition suggests that the components within each QAE-cellulose group are very closely related.

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 Amino acids as biomarkers of phase сomposition of gallstones

2020 ◽  
Vol 10 ◽  
pp. 22-30
Author(s):  
O. Ye. Amosova ◽  
◽  
Е. V. Mashina ◽  
S. N. Shanina
Keyword(s):  
Amino Acids ◽  
Phase Composition ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Gallstone Disease ◽  
Komi Republic ◽  
Protein Component ◽  
Isoleucine Leucine ◽  
The Difference

Gallstone disease (cholelithiasis) remains one of the most common gastroenterological diseases worldwide. The formation of gallstones has not been fully studied due to the latent course of the initial stage of gallstone disease. The composition of gallstones is diverse. Among the substances present in gallstones, the least studied is the protein component, the structural units of which are amino acids. In this connection, the main goal of the study was to identify patterns of changes in the amino acid composition of gallstones of various phase compositions. The objects of the study were 23 samples of gallstones belonging to residents of the Komi Republic. Data analysis was carried out by statistical one-dimensional and multidimensional methods. The statistical analysis, used in this work to study pathogenic formations in the human body, revealed qualitatively new, previously unremarked features of the amino acid composition of gallstones, which indicated the difference in the protein component and its relationship with the phase composition of gallstones. According to the results of cluster analysis by the contents of all amino acids, the studied gallstones were grouped into three different phase compositions of the type — cholesterol, cholesterol with a mineral component, and pigment. The Mann-Whitney and Student’s criteria established that all three types of gallstones were statistically significantly (p <0.05) pairwise different in the contents of alanine, valine, isoleucine, leucine, proline, phenylalanine, aspartic and glutamic acid. The lowest contents of the amino acids were determined in cholesterol gallstones, the highest — in pigment ones. The multidimensional method of classification trees also revealed individual amino acids phenylalanine, proline, leucine, according to which gallstones of different phase compositions were clearly separated by type. Based on the results obtained by statistical methods, special attention should be paid to Phenylalanine acid most clearly compared gallstones of different phase composition in comparison with others. The established relationships can be used to predict the type of cholelithiasis, to solve the problem of gallstones formation and metaphylaxis.

scholarly journals The Amino Acid Composition of Keratins II. The Amino Acid Composition of a Keratin Derivative Extracted From Wool With Alkaline Thioglycollate Solution

1955 ◽  
Vol 8 (1) ◽  
pp. 114 ◽  
Author(s):  
DH Simmonds
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Amino Acid Composition ◽  
Aspartic Acid ◽  
Acid Composition ◽  
Protein Fraction ◽  
Protein Component ◽  
Single Peak ◽  
Amide Nitrogen

The amino acid composition of a protein component of Merino 64's quality wool, which moves as a single peak on electrophoresis in alkaline thioglycollate solutions, has been determined. The results, which are summarized in Table 1, show that the purified protein fraction contains more aspartic acid, glutamic acid, leucine, lysine, and amide nitrogen, and less cystine, proline, serine, and tryptophan, than the parent wool from which it was extracted.

scholarly journals Silkmoth chorion proteins. Their diversity, amino acid composition, and the NH-terminal sequence of one component

1978 ◽  
Vol 253 (4) ◽  
pp. 1305-1314
Author(s):  
J.C. Regier ◽  
F.C. Kafatos ◽  
K.J. Kramer ◽  
R.L. Heinrikson ◽  
P.S. Keim
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Terminal Sequence ◽  
Silkmoth Chorion

scholarly journals Amino acid production in isolated rat liver mitochondria

1973 ◽  
Vol 134 (2) ◽  
pp. 431-436 ◽  
Author(s):  
W. Ferdinand ◽  
W. Bartley ◽  
V. Broomhead
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Lipid Hydroperoxide ◽  
Liver Mitochondria ◽  
Cysteic Acid ◽  
Rat Liver Mitochondria ◽  
Isolated Mitochondria ◽  
Selective Retention

Amino acid analyses of mitochondrial membranes are compared with the amino acid composition of whole mitochondria (Alberti, 1964) and found to be very similar except in the cystine content. The composition of the endogenous amino acids found in freshly prepared mitochondria has been established and shown to differ considerably from the amino acid composition of membranes or whole mitochondria. The amino acids produced during anaerobic incubation of mitochondria at pH7.4, on the other hand, resemble the membrane in composition, supporting the view that neutral proteinase activity is responsible for their appearance. Aerobic incubation produces a similar pattern of amino acids except that amino acids such as proline, serine, asparagine, glutamic acid and glutamine, which can be metabolically utilized under aerobic conditions, are present to a smaller extent. The presence of large relative concentrations of endogenous taurine, cysteic acid and oxidized glutathione and the accumulation of taurine during incubation is found. The selective retention of taurine and cysteic acid within the mitochondria is established. It is proposed that the first step in the degeneration of isolated mitochondria results from lipid hydroperoxide accumulation caused by the lack of glutathione reductase in isolated mitochondria.

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.

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