Purification of the sixth and seventh component of human complement without loss of hemolytic activity

E. R. Podack, W. P. Kolb, H. J. Mueller Eberhard

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42 Scopus citations

Abstract

Procedures for the isolation of the human complement proteins C6 and C7 have been described. These procedures allow isolation of the two proteins without any loss of hemolytic activity. Apparent activity gains of 160% and 140% were observed for C6 and C7, respectively, when the activity of the isolated proteins was compared with their activity in serum. The recovery of C6 was 3.5 to 11% and that of C7 was 7 to 13% of the amount present in serum. C6 has a m.w. of 128,000 and an electrophoretic mobility at pH 8.6 of -2.6 x 10-5 cm2 s-1 v-1. C7 has a m.w. of 121,000 and an identical electrophoretic mobility. With 3 x 107 assay cells, 63% hemolysis was achieved with 1 ng of C6 and 3.8 ng C7. On polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and after reduction with mercaptoethanol, C6 and C7 behaved as single polypeptide chain proteins.

Original languageEnglish (US)
Pages (from-to)263-269
Number of pages7
JournalJournal of Immunology
Volume116
Issue number2
StatePublished - Dec 1 1976

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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    Podack, E. R., Kolb, W. P., & Mueller Eberhard, H. J. (1976). Purification of the sixth and seventh component of human complement without loss of hemolytic activity. Journal of Immunology, 116(2), 263-269.