Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry

被引:171
作者
Bouley, J
Chambon, C
Picard, B [1 ]
机构
[1] INRA, Lab Croissance & Metab Muscle, Unite Rech Herbivores, F-63122 St Genes Champanelle, France
[2] INRA, Plateforme Proteom, F-63122 St Genes Champanelle, France
关键词
bovine skeletal muscle; mass spectrometry; troponin T; two-dimensional gel electrophoresis;
D O I
10.1002/pmic.200300688
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The large individual variation in meat quality seen both within and between animals is not fully understood. Consequently, our long-term goal is to identify reliable proteins which control or determine bovine meat quality. Using a proteomic approach, bovine skeletal muscle samples were analyzed by two-dimensional gel electrophoresis (2-DE) using an immobilized pH 4-7 gradient in the first dimension and mass spectrometry. We first tested the reproducibility of the method. These experiments showed slightly greater intersample than intrasample variability. In order to evaluate the type of visualized proteins in 2-DE, we initiated the construction of a protein reference map of bovine Semitendinosus muscle. In total, 129 protein spots corresponding to 75 different gene products were identified. Of these proteins, the largest portion is involved in metabolism (25.5%), cell structure (17%), cell defense (16%) and contractile apparatus (14.5%). One quarter of the identified proteins are represented by two or several protein spots and multiple isoforms of troponin Tare present. Peptide mass fingerprint results indicate that these isoforms are partly generated by alternative splicing. The data presented here are an important step for further proteome analyses on bovine muscle. This may lead to progress in understanding the mechanisms controlling postmortem muscle metabolism and meat quality.
引用
收藏
页码:1811 / 1824
页数:14
相关论文
共 66 条
  • [1] BAI G, 2004, GMC GENOMICS, P4
  • [2] MYOSIN DEGRADATION FRAGMENTS IN SKELETAL-MUSCLE
    BALL, RD
    KRUS, DL
    ALIZADEH, B
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1987, 193 (01) : 47 - 56
  • [3] Effects of muscle type, castration, age and growth rate on H-FABP expression in bovine skeletal muscle
    Brandstetter, AM
    Sauerwein, H
    Veerkamp, JH
    Geay, Y
    Hocquette, JF
    [J]. LIVESTOCK PRODUCTION SCIENCE, 2002, 75 (02): : 199 - 208
  • [4] BUCHER EA, 1989, J BIOL CHEM, V264, P12482
  • [5] Differential global gene expression in red and white skeletal muscle
    Campbell, WG
    Gordon, SE
    Carlson, CJ
    Pattison, JS
    Hamilton, MT
    Booth, FW
    [J]. AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 2001, 280 (04): : C763 - C768
  • [6] Castellanos-Serra L, 2002, ELECTROPHORESIS, V23, P1745, DOI 10.1002/1522-2683(200206)23:11<1745::AID-ELPS1745>3.0.CO
  • [7] 2-A
  • [8] Quantitative and qualitative measure of intralaboratory two-dimensional protein gel reproducibility and the effects of sample preparation, sample load, and image analysis
    Choe, LH
    Lee, KH
    [J]. ELECTROPHORESIS, 2003, 24 (19-20) : 3500 - 3507
  • [9] Meat quality and composition of three muscles from French cull cows and young bulls
    Dransfield, E
    Martin, JF
    Bauchart, D
    Abouelkaram, S
    Lepetit, J
    Culioli, J
    Jurie, C
    Picard, B
    [J]. ANIMAL SCIENCE, 2003, 76 : 387 - 399
  • [10] GAHLMANN R, 1987, J BIOL CHEM, V262, P16122