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引用本文的文献
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The alpha 2-macroglobulin of human plasma. I. Isolation and composition.
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Cathepsin B, Cathepsin H, and cathepsin L.
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Purification and characterization of thiol proteinase inhibitor from rat liver.
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Highly phosphorylated region of chicken riboflavin-binding protein: chemical characterization and 31P NMR studies.
Biochemistry. 1984 Jan 31;23(3):569-76. doi: 10.1021/bi00298a027.
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Human plasma alpha-cysteine proteinase inhibitor. Purification by affinity chromatography, characterization and isolation of an active fragment.
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Cystatin-like cysteine proteinase inhibitors from human liver.
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Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum.
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Human plasma alpha 1- and alpha 2-thiol proteinase inhibitors strongly inhibit Ca-activated neutral protease from muscle.
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Limited autolysis reduces the Ca2+ requirement of a smooth muscle Ca2+-activated protease.
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Limited autolysis of Ca2+-activated neutral protease (CANP) changes its sensitivity to Ca2+ ions.
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