Determination of specific radioactivity of amino acids in proteins directly on polyacrylamide gels: an application to L-leucine

Journal Article · Fri May 07 04:00:00 EDT 1976 · Anal. Biochem.; (United States)

DOI:https://doi.org/10.1016/0003-2697(76)90569-8· OSTI ID:7151918

Martin, A F; Prior, G; Zak, R

A method has been developed for determination of the specific radioactivity of L-leucine in different proteins or protein subunits which have been separated by polyacrylamide gel electrophoresis. After electrophoresis, the proteins are visualized by staining with Coomassie Brilliant Blue R, and the desired bands are excised and hydrolyzed with hydrochloric acid. In one aliquot of the hydrolysate, the radioactivity is determined, and in another, the amino acid concentration. For this purpose, we have employed an isotope dilution procedure, using the aminoacyl synthetase reaction. With this technique, 100--1500 picomol of a single amino acid can be detected.

• Research Organization: Univ. of Chicago
• OSTI ID: 7151918
• Journal Information: Anal. Biochem.; (United States), Journal Name: Anal. Biochem.; (United States) Vol. 72:1/2; ISSN ANBCA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
ACRYLAMIDE
AMIDES
AMINO ACIDS
CARBOXYLIC ACIDS
COLLOIDS
DISPERSIONS
ELECTROPHORESIS
GELS
ISOTOPE APPLICATIONS
ISOTOPE DILUTION
LEUCINE
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PROTEINS
RADIOACTIVITY
RADIOASSAY
SEPARATION PROCESSES
TRACER TECHNIQUES