scholarly journals The hydrazinolysis of insulin, lysozyme, wool proteins and wool

1958 ◽  
Vol 68 (3) ◽  
pp. 482-486 ◽  
Author(s):  
J. H. Bradbury
Keyword(s):  
Wool Proteins

scholarly journals The Isolation and Properties of Some Soluble Proteins From Wool

1964 ◽  
Vol 17 (2) ◽  
pp. 548 ◽  
Author(s):  
JM Gillespie ◽  
PJ Reis ◽  
PG Schinckel
Keyword(s):  
Amino Acids ◽  
Electron Micrographs ◽  
Soluble Proteins ◽  
Sulphur Content ◽  
Rate Of Growth ◽  
Wool Proteins

The proteins in wools of increased sulphur content, grown during abomasal infusions of casein and sulphur-containing amino acids, have been compared with those from control wools from the same sheep. It has been found that casein. methionine, or cysteine administered directly into the abomasum of the sheep, besides increasing the rate of growth of wool, greatly altered the composition of the wool proteins. The proportion of the high-sulphur proteins in wool was increased and within the group of high-sulphur proteins there was increased formation of the components richer in sulphur. No change other than the expected decrease in relative amount can be detected with the low-sulphur proteins. In electron micrographs of the test wool increased amounts of osmiophilic material can be seen in the para segment of the fibre.

scholarly journals Extraction of Reduced Wool Proteins by Solutions of Salts

1969 ◽  
Vol 22 (4) ◽  
pp. 1081 ◽  
Author(s):  
JA Maclaren ◽  
DJ Kilpatrick
Keyword(s):  
Aqueous Solution ◽  
Solvent System ◽  
Disulphide Bonds ◽  
Wool Proteins

It has been shown earlier that the disulphide bonds in wool fibres are reduced specifically and almost quantitatively in aqueous solution using toluene-w-thiol (Maclaren 1962) or tributyl phosphine (Sweetman and Maclaren 1966; Maclaren, Kilpatrick, and Kirkpatrick 1968). The next step was to find a suitable solvent system to extract the proteins from the reduced fibre.

Immunological Studies on Wool Proteins

1968 ◽  
Vol 21 (4) ◽  
pp. 815 ◽  
Author(s):  
R Frater
Keyword(s):  
Rabbit Antiserum ◽  
Double Diffusion ◽  
Immunological Methods ◽  
Considerable Heterogeneity ◽  
Agarose Gels ◽  
Wool Proteins

Immunological methods were used to study the heterogeneity of a major low-sulphur protein isolated from wool. Rabbit antiserum to the purified protein was prepared and by the use of double diffusion in agarose gels, considerable heterogeneity of the protein was demonstrated.

scholarly journals Studies on the Inhibition of Synthesis of the Tyrosine-rich Proteins of Wool

1975 ◽  
Vol 28 (4) ◽  
pp. 331 ◽  
Author(s):  
MJ Frenkel ◽  
JM Gillespie ◽  
PJ Reis
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Intravenous Injection ◽  
Intravenous Infusion ◽  
Abomasal Infusion ◽  
Partial Suppression ◽  
Wool Proteins

Three treatments known to produce weak wool were imposed on sheep, and the effects on the synthesis of high-tyrosine wool proteins were noted. The treatments were: intravenous infusion of the amino acid mimosine (a potential chemical defleecing agent), intravenous injection of the synthetic steroid Opticortenol (dexamethasone-21-trimethylacetate), and the abomasal infusion of methionine into sheep consuming a diet of wheat. All three treatments caused a partial suppression of hightyrosine protein synthesis. The inhibition caused by mimosine could not be prevented by the simultaneous infusion of tyrosine or phenylalanine, suggesting that in this system mimosine is not acting as a tyrosine antagonist.

New anionic surface-active agent derived from wool proteins for hair treatment

2010 ◽  
Vol 115 (3) ◽  
pp. 1461-1467 ◽  
Author(s):  
Clara Barba ◽  
Sonya Scott ◽  
Rob Kelly ◽  
Jose Luis Parra ◽  
Luisa Coderch
Keyword(s):  
Surface Active Agent ◽  
Active Agent ◽  
Anionic Surface Active Agent ◽  
Surface Active ◽  
Wool Proteins ◽  
Anionic Surface

scholarly journals Studies on the high-sulphur proteins of reduced Merino wool. Amino acid sequence of protein SCMKB-IIIB4

1971 ◽  
Vol 123 (2) ◽  
pp. 201-210 ◽  
Author(s):  
L. S. Swart ◽  
T. Haylett
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Complete Amino Acid Sequence ◽  
Merino Wool ◽  
The Third ◽  
Wool Proteins

The complete amino acid sequence of protein SCMKB-IIIB4 is presented. It is closely related to the sequence of protein SCMKB-IIIB3 (Haylett, Swart & Parris, 1971) differing in only four positions. The peptic and thermolysin peptides of protein SCMKB-IIIB4 were analysed by the dansyl–Edman method (Gray, 1967) and by tritium-labelling of C-terminal residues (Matsuo, Fujimoto & Tatsuno, 1966). This protein is the third member of a group of high-sulphur wool proteins with molecular weight of about 11400. It consists of 98 residues and has acetylalanine and carboxymethylcysteine as N- and C-terminal residues respectively.

scholarly journals Wool Proteins of New Zealand Romney Sheep

1987 ◽  
Vol 40 (1) ◽  
pp. 1 ◽  
Author(s):  
JL Woods ◽  
DFG Orwin
Keyword(s):  
New Zealand ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Wool Proteins

Proteins extracted from the wool of 65 Romney ewes were analysed qualitatively by one- and twodimensional polyacrylamide gel electrophoresis. Romney wool proteins could be classified into the iow-sulfur, high-sulfur, and high-tyrosine protein groups described for wool from other breeds.

The extent of reduction of wool proteins by thiols

1962 ◽  
Vol 15 (4) ◽  
pp. 824 ◽  
Author(s):  
JA Maclaren
Keyword(s):  
Dilute Solutions ◽  
Effective Agent ◽  
Merino Wool ◽  
Wool Proteins

The extent of reduction of disulphide groups in Merino wool by dilute solutions of thiols in aqueous alcohols at 20 �C has been studied by carboxymethylation of the reduced wool and estimation of the residual disulphide in the product. The wool fibres remain intact throughout the process. Under these conditions toluene-ω-thiol was the most effective agent giving 93% reduction in 2 days, and more than 99% reduction by repeated reduction-carboxymethylation cycles. With Lincoln wool 100% reduction was achieved.

scholarly journals Amino acid sequences of peptides from a tryptic digest of a urea-soluble protein fraction (U.S.3) from oxidized wool

1967 ◽  
Vol 102 (3) ◽  
pp. 801-814 ◽  
Author(s):  
M. C. Corfield ◽  
J. C. Fletcher ◽  
A. Robson
Keyword(s):  
Amino Acid ◽  
Cation Exchange ◽  
Protein Fraction ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Paper Electrophoresis ◽  
Amino Acid Sequences ◽  
Tryptic Digest ◽  
Parent Protein ◽  
Wool Proteins

1. A tryptic digest of the protein fraction U.S.3 from oxidized wool has been separated into 32 peptide fractions by cation-exchange resin chromatography. 2. Most of these fractions have been resolved into their component peptides by a combination of the techniques of cation-exchange resin chromatography, paper chromatography and paper electrophoresis. 3. The amino acid compositions of 58 of the peptides in the digest present in the largest amounts have been determined. 4. The amino acid sequences of 38 of these have been completely elucidated and those of six others partially derived. 5. These findings indicate that the parent protein in wool from which the protein fraction U.S.3 is derived has a minimum molecular weight of 74000. 6. The structures of wool proteins are discussed in the light of the peptide sequences determined, and, in particular, of those sequences in fraction U.S.3 that could not be elucidated.

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