Skip to main content

Effect of the Ph in the Conformation and Activity of the Acid Protease From Aspergillus saitoi

Buy Article:

$55.00 plus tax (Refund Policy)

The circular dichroism spectrum in the far UV-region (190-240 nm) indicates that the acid protease from Aspergillus saitoi contains appreciable amounts of beta-sheet. The structure-activity relationship of the protein is studied as a function of the pH.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: acid protease; aspergillus saitoi; cathepsins d e; gastricsin; pepsin; pepsinlilke acid proteases; renin

Document Type: Review Article

Publication date: 2001-04-01

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more