[Search for new products of gene expression in human cardiac muscle. Microsequencing of proteins after two-dimensional electrophoresis].
Proteins of the human heart muscle were studied using modified two-dimensional electrophoresis. After separation, proteins were electroblotted onto Immobilon P membranes and several protein spots were used for microsequencing analysis. In most cases the proteins analyzed have blocked N-terminal amino acids. In order to study the primary structure of these proteins, hydrolysis in situ by trypsin followed by reversed-phase HPLC and microsequencing of the resulting peptides were performed. Four protein were identified in 8 analyzed fractions, specifically myosin light chain 1 (MLCl-V/sB), fatty-acid binding protein (heart isoform), alpha (B)-crystallin and alpha-tropomyosin. Amino acid sequences of two proteins were not found among human amino acid sequences collected in SWISSPROT bank (v. 21).
Laptev
A V
AV
Shishkin
S S
SS
Egorov
Ts A
TsA
Kovalev
L I
LI
Tsvetkova
M N
MN
Galiuk
M A
MA
Musaliamov
A Kh
AKh
Efimochkin
A S
AS
D000595:Amino Acid Sequence; D015153:Blotting, Western; D015180:Electrophoresis, Gel, Two-Dimensional; D015870:Gene Expression; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009206:Myocardium / Q000378:metabolism*; D017421:Sequence Analysis
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