The major protein expression profile and two-dimensional protein database of human heart.

The construction of a two-dimensional protein database of the human heart is presented. The database contains information on about 300 abundant proteins of human myocardial tissue, including approximately 40 proteins that were identified by different methods. Each protein was characterized according to several parameters, including molecular weight, isoelectric point, name, partial sequence, subcellular localization, and genetic as well as embryonic changes.

[Study of protein products of gene expression in cells with altered chromosome sets for genetic mapping].

Two-dimensional electrophoresis was used for analyzing proteins in hybrid cells that contained single human chromosomes (chromosome 5, chromosome 21, or chromosomes 5 and 21) against the background of the mouse genome. By comparing the protein patterns of hybrid and parent cells (about 1000 protein fractions for each kind of cell), five fractions among proteins of hybrid cells were supposedly identified as human proteins. The genes of two of them are probably located on chromosome 5, and those of other three, on chromosome 21.

[A comparative analysis of the protein composition of human skeletal and cardiac muscle by two-dimensional electrophoresis].

Using a modified O'Farrell 2DE technique, the protein composition of human skeletal muscles was compared to that of human myocardium. The variability of protein composition was analysed in nine types of skeletal muscle tissue. A number of skeletal and heart muscles proteins were identified on the electrophoregrams.

[Study of human lymphocyte proteins using two-dimensional electrophoresis].

Using O'Farrell 2DE modified method, a panel of human lymphocyte proteins have been studied. A 2-D map involving 273 fractions characterized in M(r)/pI coordinates has been developed. Some proteins were identified on the map and some comparability of experimental results to the Celis et al.

[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.