Pohl J, Pereira H A, Martin N M, Spitznagel J K
Microchemical Facility, Winship Cancer Center, Atlanta, GA.
FEBS Lett. 1990 Oct 15;272(1-2):200-4. doi: 10.1016/0014-5793(90)80484-z.
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.
我们报道了CAP37的氨基酸序列，它是一种具有抗菌和单核细胞特异性趋化活性的人中性粒细胞颗粒蛋白。CAP37是一种由222个氨基酸残基组成的单链蛋白。它有三个N-糖基化位点，分别位于天冬酰胺残基100、114和145处。某些种类的CAP37在所有三个位点都被糖基化；有些仅在天冬酰胺-114处被糖基化，其他的在天冬酰胺-114和天冬酰胺-110或天冬酰胺-145处被糖基化。CAP37与人中性粒细胞弹性蛋白酶有45%的序列同一性，与其他几种颗粒丝氨酸蛋白酶有30%-37%的同一性。尽管有这些相似之处，但CAP37不是丝氨酸蛋白酶，因为其活性位点残基丝氨酸和组氨酸被取代了。
