Abstract
A highly purified trypsin inhibitor was obtained from the oriental plant Hakuhenzu bean (Dolichos lablab) by column chromatography on DEAE-Sephadex and gel-filtration on Sephadex G-75. The purified Hakuhenzu bean trypsin inhibitor (HTI) was obtained as a chemically homogeneous protein, and was stable to heat and to enzymes such as pepsin. It shows no obvious maximum at 280nm in the ultraviolet absorption spectrum, and it contains more than 20% carbohydrate as galactose and 10% hexosamine as glucosamine. The molecular weight of this inhibitor was determined to be approximately 9, 500 by gel-filtration. The protein contained 59 residures of amino acids; Lys3, His4, Arg1, Asp8, Thr3, Ser9 Glu6, Pro5, Gly1, Ala3, 1/2Cys10, Val1, Ile1, Leu2, Tyr1, Phe1, from which a molecular weight of 6, 400 is obtained. No methionine and tryptophan were found in the amino acid composition of the inhibitor. This inhibitor showed inhibitory activity against α-chymotrypsin in addition to trypsin.
