Synthesis of a heptacontapeptide corresponding to the entire amino acid sequence of eglin C.
A heptacontapeptide corresponding to the entire amino acid sequence of eglin c was synthesized by the conventional solution method using a minimal protecting method. The synthetic eglin c exhibited a symmetrical single peak on HPLC at the same retention time as an authentic eglin c, and had the same inhibitory activity against human leukocyte elastase, cathepsin G and alpha-chymotrypsin (Ki = 6.0 x 10(-9) M, 5.5 x 10(-9) M and 2.5 x 10(-9) M, respectively) as N alpha-acetyl-eglin c synthesized genetically (Ki = 5.1 x 10(-9) M, 1.5 x 10(-8) M and 2.2 x 10(-9) M, respectively).
Okada
Y
Y
Faculty of Pharmaceutical Sciences, Kobe-Gakuin University, Japan.
Tsuboi
S
S
Nagamatsu
Y
Y
Yamamoto
J
J
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D007865:Leeches; D008969:Molecular Sequence Data; D011506:Proteins; D015842:Serine Proteinase Inhibitors / Q000138:chemical synthesis*; D015843:Serpins
D011506:Proteins; D015842:Serine Proteinase Inhibitors; D015843:Serpins; C028656:eglin proteinase inhibitors