Human cathepsin B. Application of the substrate N-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide to a study of the inhibition by leupeptin.

مواد مشابهة

• A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B and of L-arginine 2-naphthylamide catalysed by cathepsin H.
  بواسطة: Willenbrock, F, وآخرون
  منشور في: (1985)
• Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2'-dipyridyl disulphide) and with a specific synthetic substrate (N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide).
  بواسطة: Willenbrock, F, وآخرون
  منشور في: (1984)
• L-arginine recognition by yeast arginyl-tRNA synthetase.
  بواسطة: Cavarelli, J, وآخرون
  منشور في: (1998)
• Fluorimetric assays for cathepsin B and cathepsin H with methylcoumarylamide substrates.
  بواسطة: Barrett, A J
  منشور في: (1980)
• Use of glycyl-L-phenylalanine 2-naphthylamide, a lysosome-disrupting cathepsin C substrate, to distinguish between lysosomes and prelysosomal endocytic vacuoles.
  بواسطة: Berg, T O, وآخرون
  منشور في: (1994)