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

Benzer Materyaller

• 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.
  Yazar:: Willenbrock, F, ve diğerleri
  Baskı/Yayın Bilgisi: (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).
  Yazar:: Willenbrock, F, ve diğerleri
  Baskı/Yayın Bilgisi: (1984)
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  Yazar:: Cavarelli, J, ve diğerleri
  Baskı/Yayın Bilgisi: (1998)
• Fluorimetric assays for cathepsin B and cathepsin H with methylcoumarylamide substrates.
  Yazar:: Barrett, A J
  Baskı/Yayın Bilgisi: (1980)
• Use of glycyl-L-phenylalanine 2-naphthylamide, a lysosome-disrupting cathepsin C substrate, to distinguish between lysosomes and prelysosomal endocytic vacuoles.
  Yazar:: Berg, T O, ve diğerleri
  Baskı/Yayın Bilgisi: (1994)