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Ficin inhibitor

Inhibition. Since papain, ficin, and bromelain are all enzymes whose activity depends on a free SH group, it is to be expected that all thiol reagents act as inhibitors. Thus, a-halogen acids or amides and N-ethyl-maleimide irreversibly inhibit the thiol proteases. Heavy metal ions and organic mercurial salts inhibit in a fashion that can be reversed by low molecular weight thiols, particularly in the presence of EDTA which... [Pg.209]

Thiol proteinase inhibitor 90,000 Ficin, papain, cathepsin B and bromelain 45, 46... [Pg.22]

Thiol proteinase (papain) inhibitor 12,700 Papain, ficin, cathepsin B 22, 21... [Pg.22]

The inhibitor is a monomeric protein with a molecular weight of 12,500. It contains 9.3% aromatic amino acids and 50.5% polar amino acid residues but no tryptophan (Table V). It inhibits most thiol pro-teinases (cathepsin H, L, B, and C, papain, and ficin) but not serine... [Pg.90]

Chicken egg cystatin C consists of one peptide chain with a ca. 120 amino acid residues (Mr 12,700). The two isomers known differ in their isoelectric point (pi 5.6 and pi 6.5) and their immunological properties. This inhibitor inhibits cysteine endopeptidases such as ficin and papain. In fact, cathepsins B, H, and L and dipeptidyl peptidase I are also inhibited. [Pg.551]


See other pages where Ficin inhibitor is mentioned: [Pg.401]    [Pg.454]    [Pg.401]    [Pg.549]    [Pg.551]    [Pg.401]    [Pg.454]    [Pg.401]    [Pg.549]    [Pg.551]    [Pg.606]    [Pg.304]    [Pg.606]    [Pg.19]    [Pg.82]    [Pg.202]   
See also in sourсe #XX -- [ Pg.549 ]




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