Egg albumen polymorphisms in the fowl: The ovalbumin locus

Lush, I. E.

doi:10.1017/s001667230000121x

Cited by 40 publications

(8 citation statements)

References 26 publications

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“…In ovalbumin A, digestion proceeds at this bond because the carboxyl group is amidated. This difference in structure is consistent with the difference in electrophoretic mobility of the two ovalbumins (Lush, 1964). The immunological implications of this difference in primary structure depend on whether it is accompanied by a difference in conformation of the proteins.…”

Section: Communications Preparationsupporting

confidence: 73%

Proceedings of The Biochemical Society

Taugner

Hasselbach

1967

Biochemical Journal

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PROCEEDINGS OF THE BIOCHEMICAL SOCIETY kinase also occurs outside the nervous system and its subcellular distribution suggests that it may be a plasma membrane component (Michell & Hawthorne, 1965). The kinase forming triphosphoinositide, on the other hand, appears largely in the supernatant fraction (Kai, Salway, Michell & Hawthorne, 1966). Direct evidence linking diphosphoinositide and triphosphoinositide with nerve excitation is lacking. These lipids are not directly involved in sodium transport (Dawson, 1965). A number of facts suggest that they might affect the permeability of the neuronal membrane and thus the action potential, through their ability to complex with

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Section: Communications Preparationsupporting

confidence: 73%

Proceedings of The Biochemical Society

Taugner

Hasselbach

1967

Biochemical Journal

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“…(a) Starch-gel electrophoresis. Electrophoresis in starch gel at pH 5.0, as described by Lush (1964), was done on all egg white and ovalbumin samples. This allowed classification into the slower-moving or common form of ovalbumin (type A), the fastermoving form of ovalbumin (type B), or a mixture of approximately equal amounts of types A and B characteristic of the hen heterozygous for this gene.…”

Section: Characterization Of Ovalbuminmentioning

confidence: 99%

“…The discovery of a genetic variant (type B) of hen ovalbumin that can be distinguished from the more common ovalbumin (type A) by its greater anionic mobility in starch-gel electrophoresis at pH 5.0 (Lush, 1964) has provided an opportunity to examine the effect of a small structural difference on the immunological activity of this protein. We have detected a difference in the reaction of the two variants with rabbit antibodies, and defined the difference in structure between these two ovalbumins.…”

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confidence: 99%

Replacement of asparagine by aspartic acid in hen ovalbumin and a difference in immunochemical reactivity

Wiseman

Fothergill

1972

Biochemical Journal

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Two forms of hen ovalbumin that exist as genetic variants were compared by physical and immunochemical techniques. The two ovalbumins could be distinguished by electrophoretic mobility and by antisera that had been pretreated with heterologous antigen. Peptide ;maps' of chymotrypsin digests of the two ovalbumins revealed that three of the peptides were different. These were isolated and analysed. One form of ovalbumin (type B) contains the sequence: -Ser-Ser-Ala-Asp-Leu-Ser-Gly-Ile-Ala-Glu-Ser(Ser,Leu)- whereas the other form (type A) contains an asparagine residue in place of the aspartic acid residue. The -Asn-Leu-Ser- sequence of type A is not glycosylated. Chymotrypsin readily cleaved the leucine-serine bond in the asparagine-containing peptide, but not in the aspartic acid-containing variant.

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“…Starting at the application point and reading toward the anode, these bands are: component 18, ovotransferrin or conalbumin, ovomucoid, and ovalbumin (Sibley 1960, Lush 1964 R. E. Feeney pers. comm.).…”

Section: Resultsmentioning

confidence: 99%

A Comparative Study of the Egg White Proteins of Some Species of the Avian Order Gruiformes

Hendrickson

1969

Ibis

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Summary No agreement has been reached on the classification of the avian order Gruiformes as defined by Peters (1934) and Wetmore (1960). Starch gel electrophoresis of egg white proteins was therefore carried out in an attempt to obtain additional taxonomic data. Individual and intrafamilial variability was observed to be small, and the protein patterns thus seem to provide a basis for classification above the familial level. These protein patterns, together with the historically conventional characters, suggest that a relationship exists between the Rallidae, Heliornithidae, Eurypygidae, Turnicidae, and Psophiidae; and that the Gruidae and Aramidae are not far removed from this assemblage. The Aramidae are thought to occupy a separate but intermediate position between the Gruidae and the rail‐like assemblage. The Otididae have a very different pattern which, together with the unusual combination of classical characters, suggests that the bustards should be removed from the order. The insufficient sampling from the Cariamidae and Rhynochetidae does little to clarify their systematic positions.

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Egg albumen polymorphisms in the fowl: The ovalbumin locus

Cited by 40 publications

References 26 publications

Proceedings of The Biochemical Society

Proceedings of The Biochemical Society

Replacement of asparagine by aspartic acid in hen ovalbumin and a difference in immunochemical reactivity

A Comparative Study of the Egg White Proteins of Some Species of the Avian Order Gruiformes

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