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. 2005 Aug;73(8):4823–4833. doi: 10.1128/IAI.73.8.4823-4833.2005

TABLE 2.

Identification of neutrophil protease cleavage products of proHD5 in urethral lavagesd

Protease HD5 peptidea Cleavage siteb Expected masse Patient Detected masse Deviation (%)
EL, PR 53-94 S52*A53 4,610.27 ND ND
EL, PR 56-94 R55*T56 4,269.8c NGU2533 4,255 0.33
CT2192 4,250 0.37
CT2309 4,254 0.35
GC2403 4,288 0.42
EL, PR 57-94 T56*S57 4,168.74 N2361 4,136 0.77
GC2414 4,150 0.43
EL 62-94 A61*R62 3,738.32c GC2182 3,755 0.45
GC2403 3,741 0.08
EL 64-94 A63*T64 3,511.05c CT2192 3,517 0.17
CT2309 3,517 0.17
GC2182 3,506 0.14
GC2403 3,518 0.19
GC2414 3,518 0.19
a

Peptides (aa) identified by N-terminal sequencing and/or MALDI analysis.

b

Amino acids and their positions flanking the cleavage site (*).

c

Masses also detected after in vitro cleavage of proHD5 with human neutrophil granule extract.

d

EL, elastase; PR, proteinase 3; ND, not detected; NGU, nongonococcal nonchlamydial urethritis; CT, chlamydial urethritis; GC, gonococcal urethritis; N, normal (healthy).

e

Masses (expected and detected) are reported in daltons.