Amino acid sequence analysis of the proteolytic cleavage products of the bovine immunodeficiency virus Gag precursor poylypeptide

Bovine immunodeficiency virus Gag proteins were purified from virions, and their amino acid sequences and molecular masses were determined. The matrix, capsid, and nucleocapsid (MA, CA, and NC, respectively) and three smaller proteins (p21, p3, and p2) were found to have molecular masses of 14.6. 24...

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Bibliographic Details
Published in:Journal of virology 1994-11, Vol.68 (11)
Main Authors: Tobin, G.J, Sowder, R.C. II, Fabris, D, Hu, M.Y, Battles, J.K, Fenselau, C, Henderson, L.E, Gonda, M.A
Format: Article
Language:English
Subjects:
LENTIVIRINAE
PEPTIDE
PEPTIDOS
PESO MOLECULAR
POIDS MOLECULAIRE
PROTEINAS
PROTEINE
VIRUS DE LOS ANIMALES
VIRUS DES ANIMAUX
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Summary:Bovine immunodeficiency virus Gag proteins were purified from virions, and their amino acid sequences and molecular masses were determined. The matrix, capsid, and nucleocapsid (MA, CA, and NC, respectively) and three smaller proteins (p21, p3, and p2) were found to have molecular masses of 14.6. 24.6, and 7.3 and 2.5, 2.7, and 1.9 kDa, respectively. The order of these six proteins in the Gag precursor, Pr53gag, is NH2-MA-p2L-CA-p3-NC-p2-COOH. In contrast to other retroviral MA proteins, the bovine immunodeficiency virus MA retains its N-terminal methionine and is not modified by fatty acids. In addition, the bovine immunodeficiency virus NC migrates as a 13-kDa protein in denaturing gel electrophoresis; however, its molecular mass was determined to be 7.3 kDa
ISSN:0022-538X
1098-5514