ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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 (ID50) 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 (Ki) 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.2000.tb15960.x
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