The haemoglobin systems of the bloodworms Glycera dibranchiata and G. americana. Oxygen binding properties of haemolysates and component haemoglobins
Roy E. Weber(Aarhus University), Celia Bonaventura(Duke University), Joseph Bonaventura(University of Essex), Bolling Sullivan(Duke Medical Center)
Comparative Biochemistry and Physiology Part B Comparative Biochemistry
January 1, 1977
Cited by 16
Related Papers
Blood Flow Regulation by <i>S</i> -Nitrosohemoglobin in the Physiological Oxygen Gradient
|Science|1997|1.1k
Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
|Proteins Structure Function and Bioinformatics|1994|397
Crystal structure of deoxygenated <i>limulus polyphemus</i> subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation
|Protein Science|1993|307
Ascaris haemoglobin is a nitric oxide-activated ‘deoxygenase’
|Nature|1999|219