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Purification and Characterization of Low Molecular Weight Kininogen from Pig Plasma
Author(s) -
Lee J.J.,
Tzeng S.S.,
Jiang S.T.
Publication year - 2000
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2000.tb15960.x
Subject(s) - kininogen , chemistry , cathepsin b , cathepsin , papain , calpain , trypsin , biochemistry , proteolysis , high molecular weight kininogen , cathepsin l , chymotrypsin , autolysis (biology) , molecular mass , microbiology and biotechnology , chromatography , enzyme , kallikrein , biology
A cysteine proteinase inhibitor from pig plasma with a molecular weight (MW) of 55 kDa, purified to electrophoretical homogeneity, inhibited μ‐ and m ‐calpains, cathepsins B, L, and L‐like, and papain, but did not inhibit trypsin, β‐chymotrypsin, and cathepsin D. The purified inhibitor was stable at pH 3.0 to 10.5. The amounts for 50% inactivation (ID 50 ) of papain, cathepsins B, L, and L‐like, μ‐ and m‐calpains were 10.55, 12.91, 2.18, 2.18, 30.91, and 29.27 nM, while the inhibition constant (K i ) for cathepsins B, L, L‐like, and X, and μ‐ and m‐calpains were 1.1, 0.64, 63.33, 8.19, 26, and 23.57 nM, respectively. It could inhibit the proteolysis of mackerel myosin heavy chain caused by purified cathepsin L‐like at 55 °C. Based on the MW, stability and specificity, it was identified as L‐kininogen.