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Michinari YOKOHAMA Takeshi MASUDA Takashi AMANO Hiroki HIRAYAMA Takashi MANABE 《Animal Science Journal》2004,75(5):401-405
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. 相似文献
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