| Literature DB >> 952923 |
A Helenius, C H von Bonsdorff.
Abstract
After Triton X-100 delipidation and subsequent Triton X-100 removal in a sucrose gradient the membrane protein spikes of Semliki Forest virus remained soluble in aqueous buffers. It was shown they were present as octameric complexes with a molecular weight of 95-10(4) and that they contain less than 4% lipid and detergent by weight. In electron microscopy after negative staining they appeared as "rosette"-shaped particles. Part of the protein could also be found associated in ordered paracrystalline arrays.Entities:
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Year: 1976 PMID： 952923 DOI： 10.1016/0005-2736(76)90421-1
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002