The 45-kilodalton protein of cytomegalovirus (Colburn) B-capsids is an amino-terminal extension form of the assembly protein.
作者： P Schenk , A S Woods , W Gibson
DOI: 10.1128/JVI.65.3.1525-1529.1991
关键词:
摘要: Intranuclear B-capsids from cytomegalovirus (strain Colburn)-infected cells contain an abundant 37-kDa assembly protein, thought to be involved in capsid formation, and three minor protein constituents (i.e., 45, 39, 38 kDa) that are immunologically structurally related the protein. In experiments reported here, antisera produced against synthetic peptides were used conjunction with chemical cleavage examine structural relationship of these proteins more detail. Results verify carboxyl end 39-kDa precursor is lost during maturation suggest 38-kDa may a processing intermediate. It shown 45-kDa coterminal mature at its but differs by predicted 115-amino-acid extension amino terminus. addition, evidence presented has 48-kDa 47-kDa putative intermediate which have same carboxy-terminal sequences undergo maturational events as those A working model considering presented.
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