Chemical modification of enzymes I. Two-step cross-linking of bovine pancreatic ribonuclease
- 1 September 1975
- journal article
- research article
- Published by Elsevier in Journal of Molecular Catalysis
- Vol. 1 (1) , 3-12
- https://doi.org/10.1016/0304-5102(75)80002-2
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Stabilization of Bacillus subtilis α-amylase by amino group acylationBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- Stabilization of glycogen phosphorylase by reductive alkylation with aliphatic aldehydesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- Effect of acetylation of Bacillus subtilis α-amylase on the kinetics of heat inactivationBiochimica et Biophysica Acta (BBA) - Enzymology, 1973
- N‐ACYLSUCCINIMIDES AS ACYLATING AGENTS FOR PROTEINS: THE SELECTIVE ACYLATION OF LYSINE RESIDUESInternational Journal of Peptide and Protein Research, 1972
- Bifunktionelle Reagentien zur Quervernetzung von ProteinenAngewandte Chemie, 1971
- Heavy atom-labelled derivatives of bovine pancreatic ribonuclease: I. specific reactions of ribonuclease with N-acetylhomocysteine thiolactone and silver ionJournal of Molecular Biology, 1969
- The Thiolation of RibonucleaseBiochemistry, 1962
- On the mechanism of enzyme action. LXX. Urea denaturation of trypsin and acyltrypsinsArchives of Biochemistry and Biophysics, 1960
- Spectrophotometric assay of bovine pancreatic ribonuclease by the use of cytidine 2′:3′-phosphateBiochemical Journal, 1960
- Formation of Peptide Bonds by Aminolysis of Homocysteine Thiolactones1Journal of the American Chemical Society, 1956