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

John E. Volanakis | Zendy; Ajit S. Bhown | Zendy; J. Bennett | Zendy; John E. Mole | Zendy

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

Author(s) -

John E. Volanakis,

Ajit S. Bhown,

J. Bennett,

John E. Mole

Publication year - 1980

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.77.2.1116

Subject(s) - proteases , serine , trypsin , peptide sequence , amino acid , biochemistry , biology , homology (biology) , microbiology and biotechnology , chemistry , enzyme , gene

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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