Avian feather keratins: Molecular aspects of structural heterogeneity
Abstract Solubilized SCM‐Keratins from feathers of a tern ( Sterna hirundo ) and turkey ( Meleagris gallopavo ) were fractionated by gel‐filtration and ion‐exchange chromatography. Tryptic peptide maps were prepared and amino‐acid compositions determined. Subsequent comparison indicated that within...
| Published in: | Journal of Experimental Zoology |
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| Main Authors: | , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
1979
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1002/jez.1402100105 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjez.1402100105 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jez.1402100105 |
| Summary: | Abstract Solubilized SCM‐Keratins from feathers of a tern ( Sterna hirundo ) and turkey ( Meleagris gallopavo ) were fractionated by gel‐filtration and ion‐exchange chromatography. Tryptic peptide maps were prepared and amino‐acid compositions determined. Subsequent comparison indicated that within each species the FKM were closely related, but separate gene products. Interspecific comparison showed species specificity. The data were compared with the homologous FKM of other species and to amino‐acid composition data of the unfractionated SCM‐KM from other tissues. These results support the proposition that feather keratins represent a family of closely related gene products. The primary function of the multiplicity of structural elements is in the macro‐molecular organization of the tissue. The monomers can self‐associate to form both the filamentous structures and an intermolecular matrix. The FKM also provide tissue specific organizational information. The chemical composition and distribution of the different FKM presumably determines the unique morphological and functional aspects of the feathers. |
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