Fluorescence technique for comparative studies of substrate-binding subsites in serine proteinases. Application to subtilisins.

Lignende værker

• Intramolecular distances between tryptophan residues and the active-site serine residue in alkaline bacterial proteinases as measured by fluorescence energy-transfer studies.
  af: Genov, N C, et al.
  Udgivet: (1983)
• A serine proteinase of an archaebacterium, Halobacterium mediterranei. A homologue of eubacterial subtilisins.
  af: Stepanov, V M, et al.
  Udgivet: (1992)
• Comparative studies of the specificities of α-chymotrypsin and subtilisin BPN′. Studies with flexible substrates
  af: Pattabiraman, T. N., et al.
  Udgivet: (1972)
• Rhodamine-based compounds as fluorogenic substrates for serine proteinases.
  af: Leytus, S P, et al.
  Udgivet: (1983)
• Effects of pH and urea on the conformational properties of subtilisin DY.
  af: Ricchelli, F, et al.
  Udgivet: (1982)