Structural relatedness between human lactotransferrin and human ceruloplasmin
- 28 September 1981
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 132 (2) , 239-242
- https://doi.org/10.1016/0014-5793(81)81169-6
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- The present state of the human lactotransferrin sequenceBiochimica et Biophysica Acta (BBA) - Protein Structure, 1981
- Internal duplication and evolution of human ceruloplasmin.Proceedings of the National Academy of Sciences, 1981
- Complete amino acid sequence of a 50,000-dalton fragment of human ceruloplasmin.Proceedings of the National Academy of Sciences, 1981
- Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. II. Amino acid sequence of the tryptic peptides.Journal of Biological Chemistry, 1980
- Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides.Journal of Biological Chemistry, 1980
- Preparation and characterization of an NH2-terminal fragment of human serum transferrin containing a single iron-binding site.Journal of Biological Chemistry, 1980
- Complete amino acid sequence of a histidine-rich proteolytic fragment of human ceruloplasmin.Proceedings of the National Academy of Sciences, 1979
- Structural studies concerning human lactotransferrin: its relatedness with human serum transferrin and evidence for internal homologyBiochimie, 1978
- A crystallographic model for azurin at 3 Å resolutionJournal of Molecular Biology, 1978
- X-ray crystal structure analysis of plastocyanin at 2.7 Å resolutionNature, 1978