Isoelectric spectrum and titration curves of Aleutian disease virus proteins

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Abstract
Three major virus‐specific proteins (Mr = 85 000, 75 000 and 25 000) were detected in purified preparations of the cell culture‐adapted Aleutian disease virus (ADV) SL3 isolate according to their molecular weight, isoelectric point and titration curve, For all structural proteins, amino acid sequence homologies were demonstrated by proteolytic peptide mapping. The virus‐induced protein Mr 75 000, detected only in lysates of infected cells, revealed a different proteolytic peptide map. It was shown that each of the structural proteins, although demonstrated to be homogeneous in molecular weight, consists of multiple species differing in their isoelectric points. Protein modifications are discussed as possible cause for the charge variations of ADV structural proteins.
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