Literature DB >> 1443566

An in vitro method for radiolabeling proteins with 35S.

J F Kalinich1, D E McClain.   

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.

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Year:  1992        PMID: 1443566     DOI: 10.1016/0003-2697(92)90425-7

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  1 in total

1.  Protein architecture of avian reovirus S1133 and identification of the cell attachment protein.

Authors:  J Martínez-Costas; A Grande; R Varela; C García-Martínez; J Benavente
Journal:  J Virol       Date:  1997-01       Impact factor: 5.103

  1 in total

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