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. 1980 Oct;36(1):115–119. doi: 10.1128/jvi.36.1.115-119.1980

Amino Acid Sequence Analysis of Reverse Transcriptase Subunits from Avian Myeloblastosis Virus

Terry D Copeland 1, Duane P Grandgenett 2, Stephen Oroszlan 1
PMCID: PMC353621  PMID: 6160262

Abstract

The NH2-terminal amino acid sequences of the α and β chains of avian myeloblastosis αβ DNA polymerase were determined by using microsequence analysis in the subnanomole range and were found to be identical up to 17 residues. The common sequence was as follows: Thr-Val-Ala-Leu-His-Leu-Ala-Ile-Pro-Leu-Lys-Trp-Lys-Pro-Asn-His-Thr-. This result provides convincing chemical evidence that the α chain is derived from the NH2-terminal region of the β chain by proteolytic cleavage, whereas the amino acid composition for these α and β subunits and p32 DNA endonuclease suggests that the latter is derived from the carboxyl-terminal region of the β chain.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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