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PMID: 6987665 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 77 ·No. 2 ·1980-02-00 ·Pages 1116-9

Volanakis JE, Bhown A, Bennett JC, Mole JE

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.

MeSH Terms
Amino Acid Sequence Autoanalysis Binding Sites Complement Activating Enzymes Complement Factor D Humans Peptide Hydrolases Serine Thrombin Trypsin
Chemicals
Serine Complement Activating Enzymes Peptide Hydrolases Trypsin CFD protein, human Complement Factor D Thrombin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Volanakis J E
Bhown A
Bennett J C
Mole J E
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.77.2.1116
Published
1980-02-00
Pages
1116-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC348435
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.77.2.1116 PMC Full Text View journal details
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