Species differences in the proteins of feathers

Harrap, B. S.; Woods, E. F.

doi:10.1016/0010-406x(67)90260-5

Cited by 55 publications

(21 citation statements)

References 14 publications

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“…They contain relatively low levels of S-carboxymethyl cysteine when compared with mammalian keratin proteins. The full extent of heterogeneity of these beak proteins has not been investigated but it is clearly limited in comparison with mammalian keratinscomparable to the situation found in feather (Harrap and Woods 1967)-and as with feather, no evidence has been found for the presence of different major protein classes equivalent to those of the mammalian keratins.…”

Section: Discussionmentioning

confidence: 99%

“…Although there is a considerable variation in the content of many amino acids when the beak proteins are compared (Table 1), this does not detract from the idea that there is a great overall similarity in composition between the members of this group of proteins. 7·8 4·9 5·4 5·5 11· 3 Asp 3·7 5·2 5·9 4·0 4·2 2·3 5·5 Thr 3·6 5·0 4·4 3·8 3·9 1·6 3·0 Ser 6·3 13·6 14·0 7·0 9·4 5·6 6·0 Glu 3·2 5·9 7·9 3·8 5·8 4·0 3·6 Pro 9·6 13·3 10·0 9·4 6·9 10·1 9·8 Gly 33·9 16·3 13·0 30·8 26·0 30·3 29·4 Ala 6·1 6·6 6·6 6·1 6·5 3·0 4'7 Val 4·0 7·3 7·8 4·7 6·5 6'7 4·0 Met 0·3 0·2 0·2 0·5 0·7 0·1 0·6 lie 1·5 4·2 3·7 1·7 2·7 1·8 2·7 Leu 5·4 7·0 7·6 5·8 6·3 8·1 2·2 Tyr 9·4 1·7 2·0 9·0 6·6 12·7 4·6 Phe 3·7 2·6 3·3 3·6 3·0 2·3 3·1 A Mean of analytical data for proteins isolated from fowl and seagull rachis, fowl and emu calamus, and fowl and turkey barbs (Harrap and Woods 1967). B Zinc-precipitable protein isolated from kookaburra claw.…”

Section: Amino Acid Composition Of Soluble Beak Proteinsmentioning

confidence: 99%

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The Proteins of the Keratin Component of Bird?s Beaks

Frenkel¹,

Gillespie²

1976

Aust. Jnl. Of Bio. Sci.

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Aust. J. BioI. Sci., 1976,29,467-79 Birds' beaks have an outer shell of hard keratin which consists almost entirely of proteins which are very rich in glycine [about 30 residues per 100 residues (residues %)], contain moderate levels of tyrosine and serine (each about 8 residues %), and which have relatively low contents of cystine (about 2·5 residues %), lysine, histidine, isoleucine and methionine.Major protein fractions in the S-carboxymethyl form isolated from the beaks of 'six different orders of birds have similar amino acid compositions, isoelectric points (pH 4·2-4·9) and molecular weights (13 000--14 500). Detailed chromatographic electrophoretic and compositional studies of the proteins of kookaburra beak reveal them to be a family of closely related proteins with only limited heterogeneity, in contrast to mammalian keratin systems.The major kookaburra beak fraction is similar in overall composition and molecular weight to fowl epidermal scale, kookaburra claw and turtle scute proteins and shows some resemblance to reptile claw protein. Beaks also contain small amounts of protein which are distinctly different from the major fraction but which resemble feather keratin proteins in composition and size.

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Section: Discussionmentioning

confidence: 99%

Section: Amino Acid Composition Of Soluble Beak Proteinsmentioning

confidence: 99%

The Proteins of the Keratin Component of Bird?s Beaks

Frenkel¹,

Gillespie²

1976

Aust. Jnl. Of Bio. Sci.

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“…It is seen (Table 4) that the amino acid composition of PK.S2 bore no obvious resemblance to component 8, a low-sulphur protein of wool nor to feather rachis extracts (Harrap and Woods 1967); relatively high glycine and methionine contents and low SCMCySH content are the characteristics ofthe epidermin (PK.S2). In view of the low sulphur content of PK.S2 it was thought that it may resemble the helical section ofthe low-sulphur proteins from wool (Crewther et al 1968) which only contain a few SCMCySH residues.…”

Section: Disoussionmentioning

confidence: 99%

“…in the sulphydryl endopeptidases from Ficus glabrata latex studied by Jones and Glazer (1970)]. The current arguments for generation of such diversity in nature are given by Hood and Talmage (1970), Hood et al (1970), and GaIly and Edelman (1970) in their studies on immunoglobulins.…”

Section: Disoussionmentioning

confidence: 99%

A Search for a Simple Keratin?The Precursor Keratin Proteins From Cow's Lip Epidermis

O'donnell¹

1971

Aust. Jnl. Of Bio. Sci.

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In searching for a material which might contain a homogeneous keratin protein as a major constituent, an examination was made of a soluble keratin precursor from cow's lip epidermis. Formic acid was used as extractant. Assessment of homogeneity was based on behaviour on DEAE-cellulose and on a consideration of the radioactively labelled peptides in a size-charge peptide map of [14C]S-carboxymethylcysteine. containing peptides from an enzyme digest. It is concluded that there is no major homogeneous keratin precursor in cow's lip epidermis and that a family of closely related proteins is present. The situation resembles that found in another a·keratin, wool. There is evidence for the existence of a fraction, amounting to 6-8% of the total protein, of higher sulphur content than the remainder of the protein both in the soluble precursor protein and in the stratum corneum.

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“…All components of a feather consist basically of keratin and have a common origin from a feather folicle (Price et al, 1991;Prum, 1999), and their amino acid profiles are remarkably similar among all their components and among species representing different orders and varied lifestyles (Harrap and Woods, 1967;King and Murphy, 1987;Murphy et al, 1990;Vincent, 1990). Therefore, if this hypothesis were correct, we would expect a negative correlation between the size and number of these structural components and the degree of fluctuating asymmetry.…”

Section: Introductionmentioning

confidence: 98%

Why do some traits show higher fluctuating asymmetry than others? A test of hypotheses with tail feathers of birds

Aparicio

Bonal

2002

Heredity

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Certain characters are more susceptible to increased fluctuating asymmetry (FA) than others. This trait-specific susceptibility has normally been attributed to different degrees of developmental stability, which could be caused by different modes of selection, functionality, or the stress experienced during the development process. Recently, it has also been suggested that the expression of FA not only depends on developmental stability, but also on the cost of growth of the trait, defined as the amount of structural components necessary to form a unit of length of a given character. In accordance with this argument, a trait with more structural components per unit of length should show lower asymmetry than a simpler one. To test this hypothesis, we examine the structure (number of barbs, barb length, and rachis width)

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Species differences in the proteins of feathers

Cited by 55 publications

References 14 publications

The Proteins of the Keratin Component of Bird?s Beaks

The Proteins of the Keratin Component of Bird?s Beaks

A Search for a Simple Keratin?The Precursor Keratin Proteins From Cow's Lip Epidermis

Why do some traits show higher fluctuating asymmetry than others? A test of hypotheses with tail feathers of birds

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