NH2-Terminal Sequence of the Clostripain and NBS Peptides of Streptococcal M5 Protein Purified in One Step by HPLC

  • B. N. Manjula
  • S. M. Mische
  • V. A. Fischetti
Part of the Experimental Biology and Medicine book series (EBAM, volume 3)

Abstract

M protein, the antiphagocytic surface molecule of the Group A streptococcus is a type specific, imiriuno logic ally diverse molecule. We have shown that the molecular characteristics of M proteins and the seven residue periodicity within their partial sequences are similar to those found in tropomyosin suggesting an alpha-helical coiled-coil structure for these molecules (1, 2). To determine if the seven residue periodicity extends throughout the molecule, sequence studies have been undertaken on a biologically active 19,000 dalton M protein fragment, namely Pep M5, isolated by limited proteolysis of the type 5 streptococci with pepsin (3).

Keywords

High Performance Liquid Chromatography Tyrosine Acetonitrile Carboxyl Fractionation 

References

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Copyright information

© The HUMANA Press Inc. 1982

Authors and Affiliations

  • B. N. Manjula
    • 1
  • S. M. Mische
    • 1
  • V. A. Fischetti
    • 1
  1. 1.The Rockefeller UniversityNew YorkUSA

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