| Autor: |
Samson AC; Department of Biochemistry and Genetics, University of Newcastle upon Tyne, U.K., Levesley I, Russell PH |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of general virology [J Gen Virol] 1991 Jul; Vol. 72 ( Pt 7), pp. 1709-13. |
| DOI: |
10.1099/0022-1317-72-7-1709 |
| Abstrakt: |
Newcastle disease virus (NDV) virions possess two proteins which react strongly with monoclonal antibody 688 following separation by high resolution two-dimensional (isoelectric focusing/SDS) PAGE and detection by Western blotting. One is the phosphorylated nucleocapsid-associated 53K [P (NAP)] protein, the other comigrates with the 36K protein detected by radiolabelling NDV-infected chick embryo fibroblasts. [35S]Cysteine/[3H]leucine dual-labelling experiments show that the 36K protein is very rich in cysteine compared to the P (NAP) protein. In the Beaudette C strain it comigrates on one-dimensional SDS-polyacrylamide gels with the matrix protein (M); however, it is resolved from the slower migrating M protein from the Ulster strain of NDV. The size, strain-specific isoelectric point, high cysteine content and antigenic relatedness to the P (NAP) protein suggest that the 36K protein is the 'V' protein of NDV, the counterpart of which is found in other Paramyxoviridae. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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