Proteomic analysis of human skeletal muscle (m. vastus lateralis) proteins: identification of 89 gene expression products.
Proteins from bioptates and autoptates of human skeletal muscle m. vastus lateralis were separated by O'Farrell two-dimensional gel electrophoresis (2DE). MALDI-TOF MS and MS/MS enabled identification of 89 protein spots as expression products of 55 genes. A modification of the O'Farrell's method including non-equilibrium electrophoresis in a pH gradient allowed detection--among major sarcomeric, mitochondrial, and cytosolic proteins--of several proteins, such as PDZ- and LIM domain-containing ones (pI > 8.70), fragments of known proteins, and a stable complex of heavy and light ferritin chains. The data underlie further studies of human skeletal muscle proteins in terms of molecular mechanisms of some physiological and pathological processes.
Kovalyova
M A
MA
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia. kovalyov@inbi.ras.ru
Kovalyov
L I
LI
Toropygin
I Yu
IY
Shigeev
S V
SV
Ivanov
A V
AV
Shishkin
S S
SS
D015180:Electrophoresis, Gel, Two-Dimensional; D015870:Gene Expression; D006801:Humans; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D018482:Muscle, Skeletal / Q000737:chemistry* / Q000378:metabolism; D040901:Proteomics; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D009124:Muscle Proteins