The Dispersion of Wool Protein by Thiols in Acid Solution

Wool suffers a loss in weight of up to 50% in 24 hr. on treatment at 50-60° C. with a salt-free aqueous solution of a particular thiol containing sufficient selected acid to bring the pH value to approximately 2. The extent of extraction depends on a number of factors such as temperature, time, pH. and the nature or concentration of thiol, acid, and any salt or other reagent which may be present. The dispersed keratin appears to undergo no appreciable chemical degradation apart from reductive fission of the disulfide bonds of the cystine residues. Apart from a small amount of residue consisting of cell membranes. wool is com pletely solubilized by treatment with concentrated aqueous thioglycollic acid at 60° C. in the absence of salts.

[1]  G. Rogers.  Electron microscopy of wool. , 1959, Journal of ultrastructure research.

[2]  L. M. Dowling,et al.  The Thermal Shrinkage of Collagen in Solutions of Electrolytes , 1958 .

[3]  J. McPhee.  The Reaction of Formaldehyde with Wool and its Effect on Digestion by Insects , 1958 .

[4]  D. Ross,et al.  The Gravimetric Estimation of Medulla in Wool , 1957 .

[5]  W. Houff,et al.  Chemical Damage in Wool , 1957 .

[6]  J. Gillespie,et al.  Keratin Derivatives Extracted From Wool with Alkaline Thioglycollate Solutions , 1955 .

[7]  R. Fraser,et al.  Microscopic observations of the alkaline-thioglycollate extraction of wool. , 1953, Biochimica et biophysica acta.

[8]  W. H. Ward.  The Molecular Size of Proteins from Several Wools Solubilized in Aqueous Urea , 1952 .

[9]  F. Bryant,et al.  A New Paper Chromatography Solvent for Amino-Acids , 1951, Nature.

[10]  H. Phillips,et al.  The action of alkalis on wool: 1. The subdivision of the combined cystine into two fractions differing in their rate and mode of reaction with alkalis. , 1945, The Biochemical journal.

[11]  J. Steinhardt,et al.  Combination of wool protein with weak acids , 1943 .

[12]  M. Harris,et al.  Chemically Modified Wools of Enhanced Stability , 1942 .

[13]  J. Steinhardt,et al.  Further investigations of the affinities of anions of strong acids for wool protection , 1942 .

[14]  J. Steinhardt.  CATALYZED HYDROLYSIS OF AMIDE AND PEPTIDE BONDS IN PROTEINS , 1941 .

[15]  L. Mizell,et al.  Role of cystine in the structure of the fibrous protein, wool , 1941 .

[16]  Kamenosuke Shinohara.  THE DETERMINATION OF THIOL AND DISULFIDE COMPOUNDS, WITH SPECIAL REFERENCE TO CYSTEINE AND CYSTINE IV. A PRECISION METHOD FOR THE DETERMINATION OF THIOL COMPOUNDS APPLIED TO THE STANDARDIZATION OF CYSTEINE HYDROCHLORIDE , 1936 .

[17]  E. Stott,et al.  The acid-combining capacity of wool , 1935 .

[18]  L. Michaelis,et al.  A STUDY ON KERATIN , 1934 .

[19]  D. J. Lloyd,et al.  The swelling of protein fibres. Part I. The swelling of collagen , 1933 .