chymotrypsin c

Leupeptin is a competitive protease inhibitor produced by actinomycetes. Leupeptin can inhibit cysteine, serine and threonine peptidases. Leupeptin inhibits serine proteinases (trypsin (Ki=3.5 nM), plasmin (Ki= 3.4 nM), porcine kallikrein), and cysteine p

Gluten exorphin C 是来源于谷朊粉的阿片肽。在 GPI 和 MVD 检测中，抑制 μ 阿片和 δ 阿片活性，IC50值分别为 40 和13.5 μM。

Eglin c (60-63) is a sequence of a peptide that has been studied for its inhibitory activity towards human leukocyte elastase, cathepsin G, porcine pancreatic elastase and alpha-chymotrypsin.

Leupeptin is a naturally occurring protease inhibitor that can inhibit cysteine, serine and threonine peptidases. Leupeptin is an organic compound produced by actinomycetes. Leupeptin inhibits serine proteinases (trypsin (Ki=3.5 nM), plasmin (Ki= 3.4 nM), porcine kallikrein), and cysteine proteinases (papain, cathepsin B (Ki = 4.1 nM), endoproteinase Lys-C). It does not inhibit α-chymotrypsin or thrombin. Leupeptin is a competitive transition state inhibitor and its inhibition may be relieved by an excess of substrate.