Proteome analysis of cashmere |
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Authors: | Michinari YOKOHAMA Takeshi MASUDA Takashi AMANO Hiroki HIRAYAMA Takashi MANABE |
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Institution: | Faculty of Bioindustry;, Graduate School of Bio-Industry, Tokyo University of Agriculture, Abashiri-shi;, Faculty of Agriculture, Tokyo University of Agriculture, Atsugi-shi;, Reproductive Biotechnology Laboratory Hokkaido Animal Research Center, Shintoku-tyo, Hokkaido;and Faculty of Science, Ehime University, Matsuyama-shi, Japan |
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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 pI 5.3 were identified as keratin type II microfibrillar (accession no. KRSHL2 ), keratin 48 k type I microfibrillar component 8c‐1 (accession no. KRSHL1 ) and cytosolic phospholipase A2 (accession no. O77793 ), 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. P02534 ) and keratin type I microfibrillar 47.6 kDa (accession no. P25690 ) (pI 5.2/42 kDa), keratin type II microfibrillar component 7C (accession no. P15241 ) and keratin typeII‐sheep (accession no. S34165 ) (pI 5.5/45 kDa), and the keratin type II microfibrillar component 5 (accession no. P25691 ) (pI 5.8–6.0/45 kDa), respectively. The three components of less than 17 kDa were identified as hair keratin type II intermediate filament (accession no. CAA51836 ) (pI 5.2) and keratin high‐sulfur matrix protein IIIB2 (accession no. P02447 ) with a different isoelectric point (pI 5.4 and 5.9), respectively. |
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Keywords: | cashmere keratin Korean native goat mass spectrometry Type IV 2-DE |
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