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Research Article

Primary Structure Polymorphism at Amino Acid Residue 72 of Human p53

, , , , &
Pages 961-963 | Received 28 Jul 1986, Accepted 06 Nov 1986, Published online: 31 Mar 2023
 

Abstract

We analyzed p53 cDNA and genomic clones from a variety of normal and transformed cells. Sequence analysis of these clones revealed that amino acid residue 72 can be an arginine, proline, or cysteine. This single codon difference results in electrophoretically distinct forms of human p53 seen in normal and transformed cells.

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