TY - JOUR
AU - KANAMORI,, Masao
AB - Abstract The reactive site peptide bond of the eggplant inhibitor against trypsin [EC 3.4.21.4] was identified by chemical modifications with 1, 2-cyclohexanedione, 2, 4, 6-trinitrobenzenesulfonic acid, acetic anhydride and glyoxal, and by sequential treatments with trypsin and carboxy-peptidase B [EC 3.4.12.3]. The inhibitor was significantly inactivated by chemical modifications of arginine residues, but was not affected by lysine modifications. Free arginine was released from the trypsin-modified inhibitor by carboxypeptidase B digestion, accompanied by a marked loss of inhibitory activity. A serine residue was newly exposed as the N-terminal amino acid of the inhibitor after modification with trypsin. The reactive site of the inhibitor against trypsin was concluded to be an arginylseryl bond. The inhibitor was completely in-activated by full reduction of its disulfide bonds. This content is only available as a PDF. Author notes 1 Present address: Department of Food Science, Faculty of Living Science, Kyoto Prefectural University, Sakyo-ku, Kyoto, Kyoto 606. © THE JOURNAL OF BIOCHEMISTRY
TI - The Reactive Site of Eggplant Trypsin Inhibitor
JO - The Journal of Biochemistry
DO - 10.1093/oxfordjournals.jbchem.a131401
DA - 1976-12-01
UR - https://www.deepdyve.com/lp/oxford-university-press/the-reactive-site-of-eggplant-trypsin-inhibitor-iRw3TV23vT
SP - 1293
EP - 1297
VL - 80
IS - 6
DP - DeepDyve
ER -