Monooxygenase activity of human hemoglobin: role of quaternary structure in the preponderant activity of the .beta. subunits within the tetramer
- 1 November 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (23), 5528-5534
- https://doi.org/10.1021/bi00318a023
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 17 references indexed in Scilit:
- Quantification of small amounts of hemoglobin in polyacrylamide gels with benzidineAnalytical Biochemistry, 1979
- Carbon-13 NMR studies of C2H5N13C bound to hemoproteins — Evidence for a different distal proteic environment in β-chains either isolated or within human hemoglobinBiochemical and Biophysical Research Communications, 1978
- Carbon monoxide binding properties of hemoglobin M IwateBiochemistry, 1976
- Characterization of Enzyme-like activity of human hemoglobin. Properties of the hemoglobin-P-450 reductase-coupled aniline hydroxylase system.Journal of Biological Chemistry, 1976
- The effect of ligand size and stereochemistry on the reactivity of the α and β chains within hemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- The Structure of a Hemoglobin Carrying Only Two Hemes*Biochemistry, 1967
- The Preparation and Properties of the Isolated α and β Subunits of Hemoglobin A*Biochemistry, 1966
- Estimation of the molecular weights of proteins by Sephadex gel-filtrationBiochemical Journal, 1964
- Standardization of hemoglobinometry II. The hemiglobincyanide methodClinica Chimica Acta; International Journal of Clinical Chemistry, 1961
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951