An aspartic acid residue at the active site of Rhodotorula glutinis acid protease
- 15 June 1974
- journal article
- Published by Wiley in FEBS Letters
- Vol. 42 (3) , 352-354
- https://doi.org/10.1016/0014-5793(74)80763-5
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- The site of diazoacetyl inhibitor attachment to acid proteinase of Aspergilius awamori — An analog of penicillopepsin and pepsinBiochemical and Biophysical Research Communications, 1972
- The Purification of the Extracellular Acid Protease ofRhodotorula glutinisK-24 and Its General PropertiesAgricultural and Biological Chemistry, 1972
- Some Physicochemical Properties and Substrate Specificity of Acid Protease of Rhodotorula glutinis K-24Agricultural and Biological Chemistry, 1972
- The Purification of the Extracellular Acid Protease of Rhodotorula glutinis K-24 and Its General PropertiesAgricultural and Biological Chemistry, 1972
- Amino acid sequence around the active site aspartic acid in penicillopepsinCanadian Journal of Biochemistry, 1970
- An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptideBiochemical Journal, 1969
- Identification of the carboxyl group of pepsin reacting with diazoacetamide derivativesBiochemical and Biophysical Research Communications, 1968
- Coloured inhibitors of pepsinBiochimica et Biophysica Acta (BBA) - Enzymology, 1968
- A reactive aspartyl residue of pepsinBiochemical and Biophysical Research Communications, 1968
- The free amino groups of insulinBiochemical Journal, 1945