Literature DB >> 6838559

Native molecular weight of adenovirus proteins: on the oligomeric structure of the fiber.

P Boulanger, C Devaux.   

Abstract

Fluorescamine-modification of amino groups was used to eliminate the influence of basic charge on the final migration position of protein's in alkaline pH polyacrylamide gradient gel electrophoresis. As applied to adenovirus structural components, this type of analysis suggested the fiber to be composed of three identical subunits. The trimeric nature of both penton base and fiber therefore displaces the problem of symmetry mismatching to penton base and surrounding hexons at each vertex of the adenovirus icosahedron.

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Year:  1983        PMID: 6838559     DOI: 10.1016/0006-291x(83)91049-5

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Human adenovirus-host cell interactions: comparative study with members of subgroups B and C.

Authors:  C Defer; M T Belin; M L Caillet-Boudin; P Boulanger
Journal:  J Virol       Date:  1990-08       Impact factor: 5.103

2.  Mutual orientation of peripentonal hexons and polypeptide subunits in the adenovirus capsid.

Authors:  E Adám; I Nász
Journal:  Arch Virol       Date:  1984       Impact factor: 2.574

  2 in total

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