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PMID: 1443566 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

An in vitro method for radiolabeling proteins with 35S.

Analytical biochemistry ·Vol. 205 ·No. 2 ·1992-09-00 ·Pages 208-12

Kalinich JF, McClain DE

Abstract

The radiolytic decomposition products of [35S]-methionine have been used to radiolabel proteins in vitro. The process occurs in a time-, temperature-, and pH-dependent manner. Maximum labeling of bovine serum albumin occurs after a 24 h incubation at 37 degrees C and pH 8.5. Once incorporated, the radiolabel cannot be removed by extended incubation at various temperatures, multiple freeze/thaw cycles, or boiling, indicating that the 35S moiety is covalently attached to the protein. A wide variety of proteins have been radiolabeled. The method is simple to perform and yields radiolabeled proteins of high specific activity.

MeSH Terms
Hydrogen-Ion Concentration In Vitro Techniques Isotope Labeling/methods Methionine/chemistry Proteins Serum Albumin, Bovine/chemistry Sulfur Radioisotopes Temperature Time Factors
Chemicals
Proteins Sulfur Radioisotopes Serum Albumin, Bovine Methionine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kalinich J F
Radiation Biochemistry Department, Armed Forces Radiobiology Research Institute, Bethesda, Maryland 20889-5145.
McClain D E
Article Info
Journal
Analytical biochemistry
Abbr.
Anal Biochem
ISSN
0003-2697
Published
1992-09-00
Pages
208-12
Language
English
Region
United States
NLM ID
0370535
Subset
IM
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