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. 1980 Feb;77(2):1116–1119. doi: 10.1073/pnas.77.2.1116

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

J E Volanakis, A Bhown, J C Bennett, J E Mole
PMCID: PMC348435  PMID: 6987665

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.

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