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October 4, 1988Biochemistry

Kinetic properties of the binding of .alpha.-lytic protease to peptide boronic acids

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Authors

CKCharles A. KettnerHeidelberg UniversityRBRoger BoneUniversity of North Carolina at Chapel Hill
David A. Agard
David A. AgardJohn Innes Centre

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Kettner et al. (1988) studied this question.

synapsesocial.com/papers/6a700d5de5469ee92be0d40ahttps://doi.org/10.1021/bi00420a017
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Also Consider

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

  1. 1Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site.1979 · 596 citations
  2. 2R-1-Acetamido-2-phenylethaneboronic acid. A specific transition-state analog for chymotrypsin1981 · 153 citations
  3. 3Nitrogen-15 NMR spectroscopy of the catalytic-triad histidine of a serine protease in peptide boronic acid inhibitor complexes1988 · 134 citations
  4. 4Inhibition of the serine proteases leukocyte elastase, pancreatic elastase, cathepsin G, and chymotrypsin by peptide boronic acids.1984 · 293 citations
  5. 5Nitrogen-15 NMR spectroscopy of hydrogen-bonding interactions in the active site of serine proteases: evidence for a moving histidine mechanism1986 · 179 citations