Molecular cloning and nucleotide sequence of a full-length cDNA for human α enolase

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Abstract

We previously purified a 48-kDa protein (p48) that specifically reacts with an antiserum directed against the 12 carboxyl-terminal amino acids of the c-myc gene product. Using an antiserum directed against the purified p48, we have cloned a cDNA from a human expression library. This cDNA hybrid-selects an mRNA that translates to a 48-kDa protein that specifically reacts with anti-p48 serum. We have isolated a full-length cDNA that encodes p48 and spans 1755 bases. The coding region is 1299 bases long; 94 bases are 5' noncoding and 359 bases are 3' noncoding. The cDNA encodes a 433 amino acid protein that is 67% homologous to yeast enolase and 94% homologous to the rat non-neuronal enolase. The purified protein has been shown to have enolase activity and has been identified to be of the α type by isoenzyme analysis. The transcriptional regulation of enolase expression in response to mitogenic stimulation of peripheral blood lymphocytes and in response to heat shock is also discussed.

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APA

Giallongo, A., Feo, S., Moore, R., Croce, C. M., & Showe, L. C. (1986). Molecular cloning and nucleotide sequence of a full-length cDNA for human α enolase. Proceedings of the National Academy of Sciences of the United States of America, 83(18), 6741–6745. https://doi.org/10.1073/pnas.83.18.6741

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