Purification and structural studies of rabbit erythrocyte cytochrome b5
- 1 September 1983
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 115 (3), 807-813
- https://doi.org/10.1016/s0006-291x(83)80006-0
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Demonstration that bovine erythrocyte cytochrome b5 is the hydrophilic segment of liver microsomal cytochrome b5Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Chemical structure of rat liver cytochrome b5 Isolation of peptides by high-pressure liquid chromatographyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Isolation of an acid protease from rabbit reticulocytes and evidence for its role in processing redox proteins during erythroid maturationBiochemical and Biophysical Research Communications, 1981
- Membrane-bound redox proteins of the murine Friend virus-induced erythroleukemia cell.The Journal of cell biology, 1979
- [8] Purification of cytochrome b5Methods in Enzymology, 1978
- Homogeneous cytochrome b5 from human erythrocytesBiochemical and Biophysical Research Communications, 1974
- Soluble cytochrome b5 from human erythrocytesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
- Amino Acid Sequence of Rabbit Liver Microsomal Cytochrome b5Journal of Biological Chemistry, 1970
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Disc electrophoresisJournal of Chemical Education, 1969