Sodium Salicylate Activates Cathepsin B But Not Cathepsin H from Rat Spleen | Zendy

Kenji Yamamoto | Zendy; Mitsue Takeda | Zendy; Yuzo Kato | Zendy

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Sodium Salicylate Activates Cathepsin B But Not Cathepsin H from Rat Spleen

Author(s) -

Kenji Yamamoto,

Mitsue Takeda,

Yuzo Kato

Publication year - 1985

Publication title -

the japanese journal of pharmacology

Language(s) - English

Resource type - Journals

eISSN - 1347-3506

pISSN - 0021-5198

DOI - 10.1254/jjp.38.215

Subject(s) - leupeptin , cathepsin b , chemistry , cathepsin o , cathepsin h , cathepsin , cysteine , cathepsin c , cathepsin s , sodium salicylate , microbiology and biotechnology , biochemistry , cathepsin l , cathepsin l1 , enzyme , biology , organic chemistry , protease

Effect of sodium salicylate (SA) and its analogues on lysosomal cysteine proteinases, cathepsins B and H, was investigated. Using a sensitive fluorometric assay, SA was shown to activate cathepsin B but not cathepsin H in the presence of cysteine. Kinetics data showed that the SA-stimulated reaction was due to a 4.5-fold decrease in Km. SA caused a decrease in the inactivation rate of cathepsin B by leupeptin and E-64. It was suggested that SA stimulates the activation process of the essential cysteine residue.

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