Primary structure and enzymatic properties of carboxypeptidase II from wheat bran
- 1 July 1987
- journal article
- research article
- Published by Springer Nature in Carlsberg Research Communications
- Vol. 52 (4), 297-311
- https://doi.org/10.1007/bf02907172
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Determination of C-terminal sequences by digestion with serine carboxypeptidases: The influence of enzyme specificityCarlsberg Research Communications, 1987
- Acid Carboxypeptidases in Grains and Leaves of Wheat, Triticum aestivum LPlant Physiology, 1986
- Subunit structure and immunological properties of wheat carboxypeptidasePhytochemistry, 1984
- Purification, crystallisation and characterisation of carboxypeptidase from wheat branFood Chemistry, 1981
- Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of .alpha.-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteasesJournal of the American Chemical Society, 1978
- [14] Cleavage at AsnGly bonds with hydroxylamineMethods in Enzymology, 1977
- Long-column meniscus depletion sedimentation equilibrium technique for the analytical ultracentrifugeAnalytical Biochemistry, 1970
- On the size of the active site in proteases. I. PapainBiochemical and Biophysical Research Communications, 1967
- Disk Electrophoresis of Basic Proteins and Peptides on Polyacrylamide GelsNature, 1962
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959