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CONTRIBUTORS:
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JOURNAL:
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Bulletin of University of Agricultural Sciences and Veterinary Medicine - Animal Sciences and Biotechnologies,
63-64(??),
311 -
316.
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YEAR:
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2007
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PUB TYPE:
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Journal Article
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SUBJECT(S):
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None
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DISCIPLINE:
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Animal Sciences
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HTTP:
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LANGUAGE:
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English
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PUB ID:
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103-437-660
(Last edited on
2007/12/20 03:51:56 US/Mountain)
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SPONSOR(S):
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ABSTRACT:
Staring from available information about amino acids properties and sequences on collagen type I chains, the aims of the study were to identify the principal property component and to analyze the similarities within and between collagens on five species. The principal component analysis applied on twenty-four amino acids properties revealed that the hydrophobic or hydrophilic character measured by Wealling et al. is more stable comparing with the other investigated properties. Similarity analysis identified similar and dissimilar within and between studied species from the viewpoint of amino acids sequences on collagen type I alpha 1 and 2 chains.
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