Isolation and characterization of genetic variants of the Kunitz soybean trypsin inhibitor

• Published in: Biochimica et Biophysica Acta - Protein structure (Netherlands) Vol. 624; no. 2
• Main Authors: Freed, R.C, Ryan, D.S. (Wisconsin Univ., Madison (USA). Dept. of Food Science)
• Format: Publication
• Language: English
• Published: 21.08.1980

Three genetically related forms of the Kunitz soybean trypsin inhibitor have been isolated by ion-exchange chromatography. The three variants have different electrophoretic mobilities and have been designated Ti('a), Ti('b) and Ti('c). An enzyme assay system was used to determine the association equilibrium constant of each variant for trypsin at pH 8.1 and values of 2. 10('9) M('-1), 2. 10('7) M('-1) and 3. 10('10) M('-1) were found for Ti('a), Ti('b) and Ti('c) respectively. The hydrolysis for each variant was also determined and found to be 4, 9 and 3 for Ti('a), Ti('b) and Ti('c), respectively