The Chemical Composition and Structure of Wool

Lindley, H.

doi:10.1007/978-1-4613-4109-3_4

Cited by 33 publications

(11 citation statements)

References 130 publications

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“…One-and two-dimensional gel electrophoreses (both IEF and NEPHGE) were performed according to Laemmli (1970) andO'Farrell et al (1975;1977), respectively. Immunoblotting was done according to Towbin et al (1979) with some modifications that facilitate the identification of individual keratins by recording photographically both the fast green and the peroxidase antiperoxidase immunoreaction staining patterns of the same blot (Woodcock-Mitchell et al, 1982;Eichner et al, 1984).…”

Section: Gel Electrophoresis and Immunoblottingmentioning

confidence: 99%

Acidic and basic hair/nail ("hard") keratins: their colocalization in upper cortical and cuticle cells of the human hair follicle and their relationship to "soft" keratins.

Lynch¹,

O’Guin²,

Hardy³

et al. 1986

The Journal of Cell Biology

349

227

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Abstract. Although numerous hair proteins have been studied biochemically and many have been sequenced, relatively little is known about their in situ distribution and differential expression in the hair follicle. To study this problem, we have prepared several mouse monoclonal antibodies that recognize different classes of human hair proteins. Our AE14 antibody recognizes a group of 10-25K hair proteins which most likely corresponds to the high sulfur proteins, our AE12 and AE13 antibodies define a doublet of 44K/46K proteins which are relatively acidic and correspond to the type I low sulfur keratins, and our previously described AE3 antibody recognizes a triplet of 56K/59K/60K proteins which are relatively basic and correspond to the type II low sulfur keratins. Using these and other immunological probes, we demonstrate the following. The 10-nm filaments of the inner root sheath cells fail to react with any of our monoclonal antibodies and are therefore immunologically distinguishable from the cortex and cuticle filaments. (d) Nail plate contains 10-20% soft keratins in addition to large amounts of hair keratins; these soft keratins have been identified as the 50K/58K and 48K/56K keratin pairs. Taken together, these results suggest that the precursor cells of hair cortex and nail plate share a major pathway of epithelial differentiation, and that the acidic 44K/46K and basic 56-60K hard keratins represent a co-expressed keratin pair which can serve as a marker for hair/nail-type epithelial differentiation.

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Section: Gel Electrophoresis and Immunoblottingmentioning

confidence: 99%

Acidic and basic hair/nail ("hard") keratins: their colocalization in upper cortical and cuticle cells of the human hair follicle and their relationship to "soft" keratins.

Lynch¹,

O’Guin²,

Hardy³

et al. 1986

The Journal of Cell Biology

349

227

View full text Add to dashboard Cite

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“…The cortex consists of spindle-shaped macrofibrils that have two main structures, the microfibril and the matrix, which are distinguished by their structures and amino acid compositions. [1][2][3][4] The microfibril is a crystalline fibrous protein mainly composed of -helical proteins with low cystine content. These structures are aligned along the fiber axis and embedded in an amorphous matrix with a high cystine content consisting of disulfide (-SS-) groups.…”

Section: Introductionmentioning

confidence: 99%

Protein structural changes in keratin fibers induced by chemical modification using 2‐iminothiolane hydrochloride: A Raman spectroscopic investigation

Kuzuhara¹

2005

Biopolymers

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For the purpose of investigating in detail the influence of chemical modification using 2-iminothiolane hydrochloride (2-IT) on keratin fibers, the structure of cross-sections at various depths of white human hair, treated with 2-IT and then oxidized, was directly analyzed without isolating the cuticle and cortex, using Raman spectroscopy. In particular, the beta-sheet and/or random coil content (beta/R) and the alpha-helix (alpha) content in human hair fibers were estimated by amide I band analysis. The S-S band intensity, amide III (unordered) band intensity, and beta/R content existing from the cuticle region to the center of cortex region of virgin white human hair remarkably increased by performing the chemical modification using 2-IT. On the other hand, not only the S-S band intensity, but also S-O band intensity existing throughout the cortex region of the bleached (damaged) white human hair increased by performing chemical modification using 2-IT. In particular, beta/R content existing throughout the cortex region of the bleached white human hair decreased, while the skeletal C-C stretch (alpha) band intensity at 935 cm(-1) and the alpha content remarkably increased. This indicates a secondary structural change from the random coil form to the alpha-helix form in the proteins existing throughout the cortex region. From these experiments, we concluded that the formation of new disulfide (-SS-) groups resulting from chemical modification using 2-IT induced the secondary structural changes of proteins existing throughout the cortex region.

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“…A possible explanation is that repeating sequences of high and ultra high-sulfur proteins are responsible, for example, a repeating pentapeptide found in numerous high sulfur proteins is well known. [715]…”

Section: Discussionmentioning

confidence: 99%

Location of keratin-associated proteins in developing fiber cuticle cells using immunoelectron microscopy

et al. 2010

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Aims:To investigate the location of keratin-associated proteins (KAPs) in developing hair fiber cuticle cells using transmission electron microscopy with immunogold techniques and specific antibodies. Other studies were aimed at detecting the presence of cornified envelope proteins including involucrin and loricrin.Mateials and Methods:Polyclonal antibodies were produced in rabbits against peptides from KAPS 5.1, KAPS 10.1 ultra high-sulfur proteins.Results:The KAP proteins were found to form part of the developing exocuticle and a- layer. Cornified envelope proteins (involucrin and loricrin) were absent consistent with recent findings.Conclusions:The results have been discussed in terms of a revised model for fiber cuticle surface barriers including their role in fiber cuticle surface function.

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The Chemical Composition and Structure of Wool

Cited by 33 publications

References 130 publications

Acidic and basic hair/nail ("hard") keratins: their colocalization in upper cortical and cuticle cells of the human hair follicle and their relationship to "soft" keratins.

Acidic and basic hair/nail ("hard") keratins: their colocalization in upper cortical and cuticle cells of the human hair follicle and their relationship to "soft" keratins.

Protein structural changes in keratin fibers induced by chemical modification using 2‐iminothiolane hydrochloride: A Raman spectroscopic investigation

Location of keratin-associated proteins in developing fiber cuticle cells using immunoelectron microscopy

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