Trypsin Inhibitors of Human Serum

A fluorometric determination of trypsin-like amidase activity and activity of trypsin inhibitors in serum.

The activity of crystalline trypsin and the trypsin-like amidase activity and the activity of trypsin inhibitors in serum were measured fluorometically, with a-benzoyl--L-arginine--na phthylamide (BANA) as substrate. The method is simpler and more sensitive than the colorimetric method based on the Bratton-Marshall reaction. Serum of pancreatectomized dogs hydrolyzed BANA at a significant rate,...

Trypsin inhibitors of human serum. I. Standardization, mechanism of reaction, and normal values.

Competition among trypsin inhibitors.

The experiments presented in this paper were designed to elucidate the kinetics of action of three protein inhibitors (from pancreas, soy bean, and egg white) on trypsin, and to discover how the inhibition by these substances was related to the action of diisopropyl fluorophosphate (DFP), mercuric chloride, and calcium salts on trypsin. The most, detailed work on the protein inhibitors of tryps...

Significance of Soya Trypsin Inhibitors

Although recent evidence clearly indicates that trypsin inhibitors (TO and low protein digestibility are the major factors responsible for the pancreatic hypertrophic and growth inhibitory effects of raw soybeans, there was uncertainty regarding the biological threshold level of TI at which these biological effects occur. To obtain such data, dehulled defatted flakes (10% dietary protein) conta...

Human plasma and serum trypsin-like esterase activity.

A spectrophotometric method using benzoyl arginine ethyl ester (BAEE) is described for the assay of serum and plasma trypsin-like esterase activity. The method was used to find activities in serum and plasma (anticoagulated with oxalate and heparin) from 12 healthy males at 3 different reaction pH’s. The effects of calcium, oxalate, heparin, soybean trypsin inhibitor, ovomucoid, and heat on thi...