A　novel　trypsin-chymotrypsin　inhibitor　with　thermal　and　pH　stability,　designated　Glycv,　was　isolated　from　Glycine　max　cv.　seeds.　The　procedure　involved　ammonium　sulfate　precipitation,　ion-exchange　chromatography　on　CM-Sephadex　C-50,　affinity　chromatography　on　Affigel　blue　gel.　The　19　N-terminal　amino　acid　sequences　were　determined　to　be　EYSKPCCDLCMCTRRCPPQ,　demonstrating　highly　homologies　with　the　sequence　of　Bowman-Birk　type　trypsin　inhibitors.　The　molecular　mass　and　isoelectric　point　of　the　inhibitor　were　estimated　by　SDS-PAGE　and　isoelectric　focusing　to　be　19.7　kD　and　5.8,　respectively.　Trypsin　could　be　completely　inhibited　by　Glycv　when　the　molar　ratio　was　8.3.　The　inhibitory　activity　of　Glycv　was　unaffected　after　exposure　to　temperatures　up　to　89　degrees　C,　as　well　as　pH　2-12.　Moreover,　the　inhibitor　Glycv　demonstrated　additional　antifungal　activity　toward　the　species　of　Fusarium　oxysporum,　Alternaria　alternate,　Physalospora　piricola,　Pythium　aphanidermatum,　Botrytis　cinerea　and　Fusarium　solani.　We　report,　for　the　first　time,　not　only　the　trypsin　inhibitor＇s　purification,　but　also　its　N-terminal　amino　acid　sequence　and　antifungal　activity　against　a　series　of　phytopathogenic　fungi.