1887

Abstract

The synthetic nonapeptide YAGAVVNDL [identical to the nine carboxy-terminal amino acids of the small subunit of herpes simplex virus (HSV)-encoded ribonucleotide reductase (RR)] was found to inhibit the RR activity induced by equine herpesvirus type 1 subtype 1 (EHV-1). Parallel experiments with HSV type 1 (HSV- l)-encoded RR established that the concentration of peptide required to inhibit 50% of the RR activity was 28 μ for both enzymes. The optimum pH for the EHV-1 enzyme was found to be between 8·0 and 8·1 which is the same as that of HSV-1 RR. By use of antisera made against peptides corresponding to different regions of the large subunit (RR1) of the HSV-1 enzyme and monoclonal antibodies directed against HSV-1 RR1 we have obtained evidence which suggests that the EHV-1 large subunit has an r of approximately 90000 and lacks the N-terminal domain which is so far unique to HSV.

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1990-06-01
2021-10-23
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