A Kunitz trypsin inhibitor of Entada scandens seeds: Another member with single disulfide bridge

Biochemical characterization ofAcacia schweinfurthiiserine proteinase inhibitor

“…The K i value obtained for ASTI can be compared with that of a trypsin inhibitor purified from Entada scandens seeds (K i of 4.9 Â 10 À9 M) 3 , indicating a very strong and potent inhibitor. The K i value of SBTI interacting with bovine trypsin is in the range of 10 .…”

“…The PIs are important tools to achieve a better understanding of fundamental principles of protein interaction and can be used to design new substances for the control of diseases and pathologic processes. PIs have drawn the attention of many researchers due to their potential medical value, for example, human immunodeficiency virus (HIV) PIs and severe acute respiratory syndrome (SARS) coronavirus PIs may be used to combat HIV and SARS virus, respectively 3 . Most PIs interact with their target proteinases by contact with the active (catalytic) site of the proteinase, resulting in the formation of a stable PI complex that is incapable of enzymatic activity 4 .…”

“…These families differ from each other in size, cysteine content and the number of reactive sites. KTIs are proteins (18-24 kDa), with one or two polypeptide chains and low Cys content, usually with four Cys residues connected by two disulphide bridges and a single reactive site 3 . Since the isolation of soybean trypsin inhibitor (SBTI) by Kunitz 11 , it has been found that PIs are widely distributed in seeds of the Leguminosae.…”

Affinity Chromatography as a Key Tool to Purify Protein Protease Inhibitors from Plants

“…HCl concentration of 0.015 M was efficient for removal from Cycas siamensis seeds inhibitor (Konarev et al, 2008). The mixture of 0.2 M Gly-HCl buffer in pH 3.0 containing 0.5 M NaCl was effective for the recovery of a Kunitz trypsin inhibitor of Entada scandens seeds (ESTI) bound the affinity chromatography on trypsin-Sepharose (Lingaraju & Gowda, 2008). Solution of 1 mM HCl was necessary to remove the trypsin inhibitors of Pithecellobium dumosum (Oliveira et al, 2007a, b; and Crotalaria pallida seeds .…”

Discoveries of Serine Protease Inhibitors from Scorpions

“…Among all classes, the Kunitz-type inhibitors are well characterized of them, possibly due to their abundance in several creatures [13,15,16]. Many studies reported that animal venoms contain Kunitz-type serine protease inhibitors [12,[17][18][19].…”