The preparation and properties of a group of proteins from the high-sulphur fraction of wool

Lindley, H.; Elleman, Thomas C.

doi:10.1042/bj1280859

Cited by 20 publications

(19 citation statements)

References 16 publications

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“…Component SCMK-B2C* was prepared from Lincoln wool as described by Lindley & Elleman (1972). Trypsin, obtained from Calbiochem, Los Angeles, Calif., U.S.A. (B grade, lot no.…”

Section: Methodsmentioning

confidence: 99%

“…Chromatography of tryptic digests of protein SCMK-B2C on DEAE-cellulose, and fractionation of peptides by high-voltage paper electrophoresis were performed as described by Lindley & Elleman (1972). Peptides on paper were located from guidestrips by the ninhydrin (0.25 %)-collidine (2%) stain or by the chlorination method of Reindel & Hoppe (1954).…”

Section: Preparation Ofpeptidesmentioning

confidence: 99%

“…These proteins are conveniently studied in a soluble form by reduction of the disulphide bonds and reaction of the resulting thiol groups with iodoacetic acid to form S-carboxy methylkerateines. A previous paper (Lindley & Elleman, 1972) has dealt with the purification and partial characterization of a group of three such proteins from wool. The present paper describes the determination of the first complete amino acid sequence of a member of this group, component SCMK-B2C (cf.…”

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confidence: 99%

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The amino acid sequence of protein SCMK-B2C from the high-sulphur fraction of wool keratin

Elleman

1972

Biochemical Journal

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1. The amino acid sequence of a protein from the reduced and carboxymethylated high-sulphur fraction of wool has been determined. 2. The sequence of this S-carboxymethylkerateine (SCMK-B2C) of 151 amino acid residues displays much internal homology and an unusual residue distribution. Thus a ten-residue sequence occurs four times near the N-terminus and five times near the C-terminus with few changes. These regions contain much of the molecule's half-cystine, whereas between them there is a region of 19 residues that are mainly small and devoid of cystine and proline. 3. Certain models of the wool fibre based on its mechanical and physical properties propose a matrix of small compact globular units linked together to form beaded chains. The unusual distribution of the component residues of protein SCMK-B2C suggests structures in the wool-fibre matrix compatible with certain features of the proposed models.

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“…Component SCMK-B2C* was prepared from Lincoln wool as described by Lindley & Elleman (1972). Trypsin, obtained from Calbiochem, Los Angeles, Calif., U.S.A. (B grade, lot no.…”

Section: Methodsmentioning

confidence: 99%

Section: Preparation Ofpeptidesmentioning

confidence: 99%

mentioning

confidence: 99%

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The amino acid sequence of protein SCMK-B2C from the high-sulphur fraction of wool keratin

Elleman

1972

Biochemical Journal

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“…The major component probably contains the SCMK-B2 subfractions A, B, and C which were resolved at acid pH, whilst the two minor bands reflect the microheterogeneity of the A, B, and C subfractions (Elleman 1972;Lindley and Elleman 1972).…”

Section: (Iii) Polyacrylamide Gel Electrophoresismentioning

confidence: 99%

“…The fraction from wool contains three sequenced components-SCMK-B2A, B2B and B2C (Elleman 1972;Lindley and Elleman 1972).…”

Section: Preparation 0/ a High-sulphur Protein Fractionmentioning

confidence: 99%

The Keratin Proteins of Wool, Horn and Hoof from Sheep

Marshall¹,

Gillespie²

1977

Aust. Jnl. Of Bio. Sci.

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Aus (. J. Bioi. Sci" 1977, 30, 389-400 This paper compares the constituent low-sulphur and high-sulphur proteins isolated from the three hard keratins-wool, horn and hoof-produced by the sheep, In general the low-sulphur protein fractions from the three keratins are similar in composition and range of molecular sizes. The same can be said for the high-sulphur protein fractions. However the relative proportions of the component proteins within each fraction vary from keratin to keratin, Hom and hoof are more similar to each other than they are to wool and, compared to wool, they contain less total high-sulphur protein and a smaller proportion of those high-sulphur protein fractions of highest sulphur content. There is a changed distribution of protein components in the low-sulphur protein fractions, and one of the wool components is apparently missing from horn and hoof.Since these keratins contain similar proteins in different proportions they should make ideal materials for studying the relation between protein composition and the mechanico-chemical properties of keratins.

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The Chemical Composition and Structure of Wool

Lindley

1977

Chemistry of Natural Protein Fibers

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The preparation and properties of a group of proteins from the high-sulphur fraction of wool

Cited by 20 publications

References 16 publications

The amino acid sequence of protein SCMK-B2C from the high-sulphur fraction of wool keratin

The amino acid sequence of protein SCMK-B2C from the high-sulphur fraction of wool keratin

The Keratin Proteins of Wool, Horn and Hoof from Sheep

The Chemical Composition and Structure of Wool

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