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The Proteins of Hair and Other Hard α-Keratins
- J. Gillespie
The mammalian hard α-keratins constitute a homologous group of epidermal appendages comprising wool, hair, hoof, the horns of cattle, goats, sheep, and rhinoceros, claw, baleen, and the quills of… Expand
Sequence of a Glycine-Rich Protein from Lizard Claw: Unusual Dilute Acid and Heptafluorobutyric Acid Cleavages
No sequence homology has been found between avian and mammalian keratin proteins and it is generally considered that they represent separate evolutionary developments. Expand
A System for the Separation of the Components of Human Blood: Quantitative Procedures for the Separation of the Protein Components of Human Plasma1a,b,c
Structure and biochemistry of mammalian hard keratin.
The structure and biological formation of hard alpha-keratin are drawn together and keratinized fibres shows considerable complexity and diversity in the structural arrangement of IFs and matrix within cortical cells. Expand
Isolation, Purification and Characterization of the Seed Globulins of Lupinus angustifolius
The three globulins of the seeds of L. angustifolius cv. Uniwhite may be satisfactorily resolved in 10 min by electrophoresis on cellulose acetate strips. These globulins, conglutins α, β and γ, vary… Expand
Menkes' kinky-hair syndrome.
Gross changes in free sulphydryl groups in hair keratin probably explain the kinky hair, and treatment of Menkes' syndrome may become possible as a result of these findings. Expand
Relation between the tyrosine content of various wools and their content of a class of proteins rich in tyrosine and glycine.
It is concluded that at least some of the hightyrosine proteins must be accommodated in an unknown region of the cortex. Expand
Proteins of the hard keratins of echidna, hedgehog, rabbit, ox and man.
The wide apparent differences in the type and relative proportions of the the low-sulphur components which comprise the major constituent proteins of the microfibrils suggest that microFibrils can tolerate a considerable variation in the constituent proteins and still produce functional structures. Expand
Influence of nutrition on the crimping rate of wool and the type and proportion of constituent proteins.
- M. E. Campbell, K. Whiteley, J. Gillespie
- Chemistry, Medicine
- Australian journal of biological sciences
- 1 August 1975
These observations can be reconciled by assuming that variations in crimp frequency are attributable solely to a combination of follicle shape and fibre length growth rate without recourse to the more generally accepted theories relating to the proportion and distribution of ortho- and paracortical cells in the firbre cortex. Expand
Effect of Sulphur Supply on the Seed Globulin Composition of Lupinus angustifolius
Studies of the protein subunit composition show that the overall molecular weight distribution of the polypeptides is independent of the level of sulphur, but under sulphur deficiency the higher molecular weight subunits do not contain the disulphide linkages normally present. Expand