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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46550

Title: Purification and Characterization of Low Molecular Weight Kininogen from Pig Plasma
Authors: J.‐J. Lee
S.‐S. Tzeng
S.‐T. Jiang
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: proteinase inhibitor
pig plasma
kininogen
protein degradation
Date: 2000
Issue Date: 2018-05-23T05:35:47Z
Publisher: Journal of Food Science
Abstract: Abstract: 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.
Relation: 68(1) pp.81-86
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46550
Appears in Collections:[食品科學系] 期刊論文

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