Double-headed protease inhibitors from black-eyed peas. I. Purification of two new protease inhibitors and the endogenous protease by affinity chromatography.

摘要: Abstract Two new double-headed protease inhibitors have been isolated from black-eyed peas. The isoinhibitors can be purified to homogeneity with greater than 90% recovery in a four-step procedure by means of sequential affinity chromatography on trypsin-Sepharose and chymotrypsin-Sepharose columns. both molecular weights near 8,000 the same NH1-terminal residue serine. Black-eyed pea chymotrypsin trypsin inhibitor (BEPCI) has an isoelectric point 5.1 inhibits simultaneously. (BEPTI) 6.5 2 molecules BEPTI binds above pH 6 but does not inhibit standard assay 10-3 M substrate. These are distinct Ventura Serido An endogenous seed peas soybean inhibitor-carboxymethylcellulose A protease-BEPCI complex ion exchange chromatography. dual physiological function inhibition protection is suggested as plausible role inhibitors.