Abstract
A trypsin/chymotrypsin inhibitor was isolated from human amniotic fluid in a homogenous form by chromatography on DEAE-cellulose, Sephadex G-100, and Con A—Sepharose. The molecular weight of the inhibitor was found to be 18,000 based on the data on polyacrylamide gel electrophoresis in presence of SDS and mercaptoethanol. The inhibitor was stable over a wide pH range (1–10.5) and was inactivated only under highly alkaline conditions. The inhibitor was found to be a glycoprotein. The mode of inhibition of trypsin as well as α-chymotrypsin was noncompetitive. The binding sites on the inhibitor for trypsin and α-chymotrypsin are different. Arginine residues formed part of the reactive center for trypsin binding.
Published Version
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