Partial amino acid sequence of human factor D:homology with serine proteases.

Academic Article

Abstract

  • Human factor D purified to homogeneity by a modified procedure was subjected to NH2-terminal amino acid sequence analysis by using a modified automated Beckman sequencer. We identified 48 of the first 57 NH2-terminal amino acids in a single sequencer run, using microgram quantities of factor D. The deduced amino acid sequence represents approximately 25% of the primary structure of factor D. This extended NH2-terminal amino acid sequence of factor D was compared to that of other trypsin-related serine proteases. By visual inspection, strong homologies (33--50% identity) were observed with all the serine proteases included in the comparison. Interestingly, factor D showed a higher degree of homology to serine proteases of pancreatic origin than to those of serum origin.
  • Authors

    Digital Object Identifier (doi)

    Author List

  • Volanakis JE; Bhown A; Bennett JC; Mole JE
  • Start Page

  • 1116
  • End Page

  • 1119
  • Volume

  • 77
  • Issue

  • 2