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Proteome analysis of whole and water‐soluble proteins in masseter and semitendinosus muscles of Holstein cows
Author(s) -
OE Mika,
OHNISHIKAMEYAMA Mayumi,
NAKAJIMA Ikuyo,
MUROYA Susumu,
SHIBATA Masahiro,
OJIMA Koichi,
KUSHIBIKI Shiro,
CHIKUNI Koichi
Publication year - 2011
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/j.1740-0929.2010.00823.x
Subject(s) - myofibril , myosin , tropomyosin , proteome , myosin light chain kinase , chemistry , biochemistry , aldolase a , sarcoplasm , triosephosphate isomerase , calsequestrin , enzyme , endoplasmic reticulum , ryanodine receptor , intracellular
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.