1887

Abstract

Summary

Bacteriophage MX-1 is a virulent DNA phage for Myxococcus. The host range includes strains of and . The phage has a sedimentation coefficient ( ) of 1145S and a density of 1.531 g/ml. By using SDS-polyacrylamide gel electrophoresis, 23 phage proteins with apparent mol. wt. between 10000 and 150000 were resolved. Gel filtration in the presence of nonionic detergent partially resolved the proteins. The fraction excluded from Sephadex G-100, fraction 1, contains two glycoproteins. Fraction 1 was resolved into three fractions (1.1, 1.2 and 1.3) by chromatography on Sephadex G-200. The glycoproteins were present in fraction 1.2; all the proteins from this fraction were derived from the phage tail. Comparison of the amino-acid, hexosamine and neutral-sugar compositions of the two glycoproteins showed that they are distinct molecular species; the smaller molecule is not a subunit of the larger. The significance of these findings is discussed and compared with the proteins of the tails of T-even phage of .

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/content/journal/jgv/10.1099/0022-1317-30-1-99
1976-01-01
2019-11-21
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-30-1-99
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