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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…
The Proteins of Hair and Other Hard α-Keratins
- J. Gillespie
X-ray diffraction analysis and electron microscopy show that these tissues have a unique arrangement of the constituent proteins, comprising intermediate filaments (IFs) traditionally termed microfibrils, surrounded by a nonfilamentous matrix of IF-associated protein (IFAP).
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.
Structure and biochemistry of mammalian hard keratin.
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.
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
Menkes' kinky-hair syndrome.
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.
A comparison of lizard claw keratin proteins with those of avian beak and claw
The major lizard claw proteins are therefore similar in size and glycine content to the proteins of avian beak and claw but differ in containing more cystine and less tyrosine, and differ in size with the lizard proteins being larger.
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.