Portal de Periódicos da CAPES

Double-headed protease inhibitors from black-eyed peas. II. Structural studies by optical absorption and circular dichroism.

1976; Elsevier BV; Volume: 251; Issue: 3 Linguagem: Inglês

10.1016/s0021-9258(17)33846-2

1083-351X

L S Gennis, C R Cantor,

Food Chemistry and Fat Analysis

Two new double-headed protease inhibitors from black-eyed peas have amino acid compositions typical of the low molecular weight protease inhibitors from legume seeds.Black-eyed pea chymotrypsin and trypsin inhibitor (BEPCI) contains no tryptophan, 1 tyrosine, and 14 half-cystines out of 83 amino acid residues per monomer.Black-eyed pea trypsin inhibitor (BEPTI) contains no tryptophan, 1 tyrosine, and 14 half-cystines out of 75 residues per monomer.The molar extinctions at 280 nm are 2770