Amino acid sequence of CAP37, a human neutrophil granule‐derived antibacterial and monocyte‐specific chemotactic glycoprotein structurally similar to neutrophil …

J Pohl, HA Pereira, NM Martin, JK Spitznagel - FEBS letters, 1990 - Wiley Online Library
J Pohl, HA Pereira, NM Martin, JK Spitznagel
FEBS letters, 1990Wiley Online Library
We report the amino acid sequence of CAP37, a human neutrophil granule protein with
antibacterial and monocyte‐specific chemotactic activity. CAP37 is a single‐chain protein
consisting of 222 amino acid residues. It has three N‐glycosylation sites, at Asn residues
100, 114 and 145. Some species of CAP37 are glycosylated at all three sites; some at Asn‐
114 alone, others at Asn‐114 and Asn‐110 or Asn‐145. CAP37 has 45% sequence identity
to human neutrophil elastase, and 30–37% identity to several other granule serine …
We report the amino acid sequence of CAP37, a human neutrophil granule protein with antibacterial and monocyte‐specific chemotactic activity. CAP37 is a single‐chain protein consisting of 222 amino acid residues. It has three N‐glycosylation sites, at Asn residues 100, 114 and 145. Some species of CAP37 are glycosylated at all three sites; some at Asn‐114 alone, others at Asn‐114 and Asn‐110 or Asn‐145. CAP37 has 45% sequence identity to human neutrophil elastase, and 30–37% identity to several other granule serine proteinases. Despite these similarities, CAP37 is not a serine proteinase because the active site residues serine and histidine are replaced.
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