A　novel　trypsin　inhibitor　with　considerable　thermal　and　pH　stability,　designated　Glytine,　was　isolated　from　seeds　of　the　Chinese　black　soybean　Glycine　max　(L.)　Merr.　The　purification　procedure　involved　ammonium　sulfate　precipitation,　ion-exchange　chromatography　on　CM-Sephadex　C-50,　gel　filtration　chromatography　on　Sephacryl　S-200HR,　and　gel　filtration　chromatography　on　POROS　HS-20.　The　20　N-terminal　amino　acid　sequences　were　determined　to　be　DEYSKPCCDLCMCTRRCPPQ,　demonstrating　close　homology　with　the　sequences　of　leguminous　trypsin　inhibitors.　The　molecular　mass　and　isoelectric　point　of　the　inhibitor　were　estimated　by　SDS-PAGE　and　isoelectric　focusing　to　be　19.9　kDa　and　6.2,　respectively.　Trypsin　could　be　completely　inhibited　by　Glytine　when　the　weight　ratio　was　1.5.　The　inhibitory　activity　of　Glytine　was　unaffected　by　exposure　to　temperatures　up　to　100　A　degrees　C,　or　within　the　pH　range　2-12.　Besides　trypsin-chymotrypsin　inhibition　activity,　Glytine　demonstrated　other　biological　activities　including　antiproliferative　activity　against　tumor　cells　including　human　liver　hepatoma　cells　Bel-7402　and　neuroblastoma　cells　SHSY5Y.　In　addition,　the　inhibitor　showed　antifungal　activity　against　Pythium　aphanidermatum,　Fusarium　oxysporum,　Alternaria　alternata　(Fr.)　Keiss,　Fusarium　solani,　and　Botrytis　cinerea.　This　study　extended　research　on　leguminous　trypsin-chymotrypsin　inhibitor　and　suggested　exploitable　potential.