Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four major components of the head are cleaved during the process of assembly, apparently after the precursor proteins have assembled into some large intermediate structure.

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

A method has been devised for the electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. The method results in quantitative transfer of ribosomal proteins from gels containing urea. For sodium dodecyl sulfate gels, the original band pattern was obtained with no loss of resolution, but the transfer was not quantitative. The method allows detection of proteins by autoradiography and is simpler than conventional procedures. The immobilized proteins were detectable by immunological procedures. All additional binding capacity on the nitrocellulose was blocked with excess protein; then a specific antibody was bound and, finally, a second antibody directed against the first antibody. The second antibody was either radioactively labeled or conjugated to fluorescein or to peroxidase. The specific protein was then detected by either autoradiography, under UV light, or by the peroxidase reaction product, respectively. In the latter case, as little as 100 pg of protein was clearly detectable. It is anticipated that the procedure will be applicable to analysis of a wide variety of proteins with specific reactions or ligands.

https://www.pnas.org/content/pnas/76/9/4350.full.pdf

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.

High resolution two-dimensional electrophoresis of proteins.

http://www.real-times.com.cn/guest/20143219541398.pdf

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

https://www.jbc.org/content/252/3/1102.full.pdf

Ulrich K. Laemmli

Papers

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

Maturation of the head of bacteriophage T4. I. DNA packaging events.

Maturation of the head of bacteriophage T4. II. Head-related, aberrant tau-particles.

Organization of the higher-order chromatin loop: specific DNA attachment sites on nuclear scaffold