Proteome analysis of whole and water-soluble proteins in masseter and semitendinosus muscles of Holstein cows.
To assess both quantitative and qualitative differences between the slow- and fast-type muscles, masseter (slow) and semitendinosus (fast) from four Holstein cows were analyzed by two-dimensional difference gel electrophoresis (2D DIGE) and mass spectrometry. The proteome analysis identified 27 spots as 20 proteins in the whole protein fraction extracted with 8 mol/L urea solution, and 16 spots were identified as 11 proteins in the water-soluble protein fraction. Two slow-type myofibrillar proteins (myosin light chain-1 slow-b and myosin light chain-2 slow), and aconitase-2 mitochondria were present at higher levels in the masseter muscle (P < 0.05). Four fast-type myofibrillar proteins (myosin light chain-1 fast, myosin light chain-2 fast, myosin light chain-3 fast and tropomyosin-1), and three enzymes of glycolytic pathway (enolase-3, aldolase-A and triosephosphate isomerase), were present at higher levels in the semitendinosus muscle (P < 0.05). Our proteome analysis showed that the composition of sarcoplasmic proteins as well as myofibrillar proteins was clearly different between slow- and fast-type muscles.
National Institute of Livestock and Grassland Science, Tsukuba, Ibaraki, Japan. mooe@affrc.go.jp
Mika
M
Oe
Mayumi
M
Ohnishi-Kameyama
Ikuyo
I
Nakajima
Susumu
S
Muroya
Masahiro
M
Shibata
Koichi
K
Ojima
Shiro
S
Kushibiki
Koichi
K
Chikuni
D000818:Animals; D002417:Cattle; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D013058:Mass Spectrometry; D008406:Masseter Muscle / Q000737:chemistry*; D008460:Meat; D009124:Muscle Proteins / Q000032:analysis* / Q000302:isolation & purification*; D018482:Muscle, Skeletal / Q000737:chemistry*; D020543:Proteome / Q000032:analysis*; D012995:Solubility; D013710:Tendons; D014867:Water
D009124:Muscle Proteins; D020543:Proteome; D014867:Water