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- W1938242955 abstract "By a mild alkaline treatment of pyocin R1, the core particle was released from the contracted sheath. After sucrose density-gradient centrifugation, core-rich fractions were treated with anti-sheath serum and by a second density-gradient centrifugation, purified core particles were isolated. Homogeneity of the preparation was confirmed by observation under the electron microscope, immuno-precipitation reaction, and sucrose density-gradient centrifugation. The core particle exhibited a sedimentation coefficient of 37S. The quaternary structure of the core consists of a single kind of subunit protein with a molecular weight of 18,000. No contamination by other proteins was detected by SDS-disc electrophoreses. Amino acid analysis revealed that the core is rich in glycine, alanine, valine, leucine, aspartic acid (or asparagine), glutamic acid (or glutamine), and serine. This amino acid composition bears some resemblance to that of T-even bacteriophage tail-core." @default.
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- W1938242955 date "1979-02-01" @default.
- W1938242955 modified "2023-09-23" @default.
- W1938242955 title "Isolation, Homogeneity, and Properties of Core Particle from Pyocin RI11" @default.
- W1938242955 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a132347" @default.
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