ROLE OF THE LYSINE, TYROSINE AND TRYPTOPHAN RESIDUES IN THE ACTIVITY OF MILK LYSOZYMES
- 1 July 1975
- journal article
- Published by Wiley in Journal of Food Science
- Vol. 40 (4) , 833-836
- https://doi.org/10.1111/j.1365-2621.1975.tb00569.x
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Enzymic and immunochemical properties of lysozyme. I. Derivatives modified at tyrosine. Influence of nature of modification on activityBiochemistry, 1969
- Nature of amino acid side chains which are critical for the activity of lysozymeBiochemistry, 1969
- Acetylation of LysozymeAgricultural and Biological Chemistry, 1968
- Acetylation of LysozymeAgricultural and Biological Chemistry, 1968
- Inhibition of Lysozyme by N-Acyl-D-glucosamine DerivativesNature, 1967
- The Oxidation by Iodine of Tryptophan 108 in LysozymeJournal of the American Chemical Society, 1967
- Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å ResolutionNature, 1965
- Purification and some properties of bovine milk lysozymeBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965
- SELECTIVE CLEAVAGE OF PEPTIDE BONDS. II. THE TRYPTOPHYL PEPTIDE BOND AND THE CLEAVAGE OF GLUCAGON1Journal of the American Chemical Society, 1958
- The guanidination of some biologically active proteinsBiochimica et Biophysica Acta, 1957