Complete amino acid sequences of three proteinase inhibitors from white sword bean (Canavalia gladiata).
Three major serine proteinase inhibitors (SBI-1, -2, and -3) were purified from the seeds of white sword bean (Canavalia gladiata) by FPLC and reversed-phase HPLC. The sequences of these inhibitors were established by automatic Edman degradation and TOF-mass spectrometry. SBI-1, -2, and -3 consisted of 72, 73, and 75 amino acid residues, with molecular masses of 7806.5, 7919.8, and 8163.4, respectively. The sequences of SBI-1 and -2 coincided with those of CLT I and II [Terada et al. (1994) Biosci. Biotech. Biochem., 58, 376-379] except only N- or C-terminal amino acid residues. Analysis of the amino acid sequences showed that the active sites of the inhibitors contained a Lys21-Ser22 against trypsin and Leu48-Ser49 against chymotrypsin, respectively. Further, it became apparent that about seven disulfide bonds were present. These results suggest that sword bean inhibitors are members of the Bowman-Birk proteinase inhibitor family.
Park
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Materials Chemistry Department, Kyushu National Industrial Research Institute, Tosu, Saga, Japan. park@kniri.go.jp
Sumi
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T
Ohba
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H
Nakamura
O
O
Kimura
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M
D000595:Amino Acid Sequence; D002853:Chromatography, Liquid; D007887:Fabaceae / Q000737:chemistry*; D008969:Molecular Sequence Data; D010946:Plants, Medicinal; D017386:Sequence Homology, Amino Acid; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D015842:Serine Proteinase Inhibitors