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Chromatographic Separation and Structural Analysis of Heq 1 Hemagglutinin

  • D. J. Bucher
  • S. S-L. Li
Part of the Topics in Infectious Diseases book series (TIDIS, volume 3)

Summary

Amino terminal analysis of the hemagglutinin polypeptides HA1 and HA2 were performed on 50-100mM quantities of protein purified from X-38 influenza vaccine (Heg1N2). A cysteine was identified at position 4 from the amino terminus of HA1 which had previously been tentatively identified as a serine residue. A chromatographic technique was developed for the separation of the hemagglutinin from nucleoprotein without reduction, thus permitting the disulfides to remain intact for further structural studies of inter and intrachain disulfides.

Cyanogen bromide cleavage was performed on the HA1 polypeptide. The fragments were separated into six fractions on Sephadex G-50 in 30% formic acid. The original amino terminal fragment was found only in fraction 1, the void volume. Two of the fractions contained at least two sequences and three fractions contained only one amino terminal sequence and were considered to be purified at this step.

Keywords

Influenza Vaccine Void Volume Cyanogen Bromide Viral Preparation Iodoacetic Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Springer-Verlag Wien 1978

Authors and Affiliations

  • D. J. Bucher
  • S. S-L. Li

There are no affiliations available

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