| Literature DB >> 6160262 |
T D Copeland, D P Grandgenett, S Oroszlan.
Abstract
The NH(2)-terminal amino acid sequences of the alpha and beta chains of avian myeloblastosis alphabeta 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 alpha chain is derived from the NH(2)-terminal region of the beta chain by proteolytic cleavage, whereas the amino acid composition for these alpha and beta subunits and p32 DNA endonuclease suggests that the latter is derived from the carboxyl-terminal region of the beta chain.Entities:
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Year: 1980 PMID: 6160262 PMCID: PMC353621 DOI: 10.1128/JVI.36.1.115-119.1980
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103