Chymotrypsin inhibitor activity in winged beans (Psophocarpus tetragonolobus)

1984 ◽  
Vol 32 (1) ◽  
pp. 163-166 ◽  
Author(s):  
Nget Hong Tan ◽  
Zubaidah H. A. Rahim ◽  
Hun Teik Khor ◽  
Kai Choo Wong
1974 ◽  
Vol 20 (3) ◽  
pp. 328-331 ◽  
Author(s):  
Julius Wenger ◽  
Marian Sundy

Abstract Serum protease inhibitor activity was assessed from the ability of the serum to inhibit casein hydrolysis by α-chymotrypsin (EC 3.4.4.5). Unmodified AutoAnalyzer equipment was used in conjunction with a fluorimetric method for dialyzable tyrosyl peptides. Serum, diluted with tris(hydroxymethyl) aminomethane buffer, was added to a chymotrypsin solution to inhibit its activity. For 72 sera, the automated method was compared with a manual determination of trypsin inhibitor capacity. Results by the two methods correlate well, supporting previous evidence that trypsin and chymotrypsin-inhibitor capacities of serum are related. The present automated method has several advantages that make it useful for clinical studies.


Sign in / Sign up

Export Citation Format

Share Document