[Structure and regulation of the assembly of bacteriophage T4 fibrillar proteins. II. Isolation and initial structural characteristics of whiskers].
A procedure for purification of bacteriophage T4 whiskers and it's monomeric subunits--gene product wac--has been developed. We have shown, that the whiskers are composed of two identical copies of gene product wac with molecular weight of 56 kDa each. The dimer of gene product wac is a highly ordered structure and it's length is about 70.0 +/- 10.0 nm, as revealed by electron microscopy. The amino acid composition of whiskers is very similar to that of watersoluble keratins. We have proposed a new term for the definition of the whiskers--the fibritin.
D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D008854:Microscopy, Electron; D011487:Protein Conformation; D013604:T-Phages / Q000032:analysis* / Q000648:ultrastructure; D014764:Viral Proteins / Q000032:analysis* / Q000302:isolation & purification; D017376:Viral Tail Proteins
D014764:Viral Proteins; D017376:Viral Tail Proteins
Struktura i reguliatsiia sborki fibrilliarnykh belkov bakteriofaga T4. II. Vydelenie i nachal'naia strukturnaia kharakteristika vorotnichkovykh niteĭ.