Chemical modification of tyrosyl and lysyl residues in goat alpha lactalbumin and the effect on the interaction with the galactosyl transferase
- 27 February 1980
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 621 (2) , 333-337
- https://doi.org/10.1016/0005-2795(80)90185-3
Abstract
No abstract availableKeywords
This publication has 5 references indexed in Scilit:
- A folding model of α-lactalbumin deduced from the three-state denaturation mechanismJournal of Molecular Biology, 1977
- Maleyl-α-lactalbumin as lactose synthetase specifier proteinBiochimica et Biophysica Acta (BBA) - Biomembranes, 1973
- Inter- and intramolecular interactions of α-lactalbumin: XII. Changes in the environment of aromatic residues in the goat proteinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- Inter- and intramolecular interactions of α-lactalbumin XI. Comparison of the “exposure” of tyrosyl, tryptophyl, and lysyl side chains in the goat and bovine proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- Inter- and Intramolecular Interactions of α-LactalbuminPublished by Elsevier ,1971