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Radioiodination and /sup 125/I-labeled peptide mapping of proteins on nitrocellulose membranes

Journal Article · · Anal. Biochem.; (United States)

A rapid procedure for generating dozens of /sup 125/I-labeled peptide maps from a protein band excised from a single lane of a sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) gel has been developed. Proteins, which can be rapidly purified by 2 X SDS-PAGE separation, are electroblotted onto nitrocellulose paper (NCP) and located by aqueous naphthol blue-black staining. All subsequent steps of radioiodination, and enzyme or chemical cleavage, are carried out on the NCP making it possible to test a variety of cleavage reagents on the same protein sample. The resultant peptidic residues, which can be separated by thin-layer electrophoresis-thin-layer chromatography (2D TLE-TLC), SDS-PAGE, or HPLC, can be used in comparative studies or they can be recovered for further structural and immunological analyses.

Research Organization:
Univ. of Montana, Missoula
OSTI ID:
6501031
Journal Information:
Anal. Biochem.; (United States), Journal Name: Anal. Biochem.; (United States) Vol. 2; ISSN ANBCA
Country of Publication:
United States
Language:
English