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- Title
Proteome analysis of cashmere.
- Authors
Yokohama, Michinari; Masuda, Takeshi; Amano, Takashi; Hirayama, Hiroki; Manabe, Takashi
- Abstract
As an analysis of the cashmere proteins by Type IV 2-DE, ten kinds of components, including three components with molecular mass 42–50 kDa whose expression level increased in the winter, were separated. In analyzing nine components of these ten using a mass spectrometer, the three components of molecular mass 70–120 kDa and pI5.3 were identified as keratin type II microfibrillar (accession no.), keratin 48 k type I microfibrillar component 8c-1 (accession no.) and cytosolic phospholipase A2 (accession no.), respectively. The three components whose expression level increased in the winter, were identified as keratin type I microfibrillar 48 kDa component 8C-1 (accession no.) and keratin type I microfibrillar 47.6 kDa (accession no.) (pI5.2/42 kDa), keratin type II microfibrillar component 7C (accession no.) and keratin typeII-sheep (accession no.) (pI5.5/45 kDa), and the keratin type II microfibrillar component 5 (accession no.) (pI5.8–6.0/45 kDa), respectively. The three components of less than 17 kDa were identified as hair keratin type II intermediate filament (accession no.) (pI5.2) and keratin high-sulfur matrix protein(accession no.) with a different isoelectric point (pI5.4 and 5.9), respectively.
- Subjects
KASHMIR goat; KERATIN; PROTEINS; MASS spectrometry; GOAT breeds
- Publication
Animal Science Journal, 2004, Vol 75, Issue 5, p401
- ISSN
1344-3941
- Publication type
Article
- DOI
10.1111/j.1740-0929.2004.00204.x