[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).