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April 1, 1995European Journal of Biochemistry

The Preparation of Catalytically Active Human Cathepsin B from Its Precursor Expressed in Escherichia coli in the Form of Inclusion Bodies

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Authors

RKRobert KuheljBiogen (United States)MDMarko DolinarUniversity of LjubljanaJPJože PungerčarJožef Stefan Institute

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Kuhelj et al. (1995) studied this question.

synapsesocial.com/papers/6a7cdead3c7b3e4c163e13echttps://doi.org/10.1111/j.1432-1033.1995.0533k.x
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Characterization of recombinant rat cathepsin B and nonglycosylated mutants expressed in yeast. New insights into the pH dependence of cathepsin B-catalyzed hydrolyses.1992 · 90 citations
  2. 2Amino acid sequence of human liver cathepsin B1985 · 83 citations
  3. 3Generation of antibody activity from immunoglobulin polypeptide chains produced in Escherichia coli.1984 · 172 citations
  4. 4Maturation of human procathepsin B. Proenzyme activation and proteolytic processing of the precursor to the mature proteinase, in vitro, are primarily unimolecular processes.1994 · 176 citations
  5. 5Proteolytic processing and glycosylation of cathepsin B. The role of the primary structure of the latent precursor and of the carbohydrate moiety for cell-type-specific molecular forms of the enzyme1992 · 97 citations