Hemoglobins and hemocyanins: comparative aspects of structure and function.
Comparative studies of protein structure and function can be quite interesting by themselves, and even more interesting when interpreted with respect to an animal's physiology. In the case of fish hemoglobins, some success in the latter has been achieved but there are still many unsolved problems. It appears that comparative physiology and biochemistry have entered an era where results from comparative studies can shed a great deal of light on biochemical mechanisms in general. The trout hemoglobin system is an example. Distinctive hemoglobins in this system are presently being used as high resolution probes of the ligand-binding mechanism. Characterization of the multiple, structurally distinct subunits of the 60S Limulus hemocyanin molecule may similarly aid in understanding its function. Our studies suggest the possibility of using Limulus hemocyanin and other hemocyanins as structural homologs and analogs of more complex macromolecular arrays. The rapid development of molecular structural data from X-ray crystallographers combined with the vast data of comparative physiology and biochemistry makes this one of the most exciting areas in present day science.
D000818:Animals; D001665:Binding Sites; D003386:Brachyura / Q000378:metabolism; D005399:Fishes / Q000097:blood; D006433:Hemocyanins / Q000032:analysis / Q000302:isolation & purification; D006454:Hemoglobins / Q000032:analysis / Q000302:isolation & purification; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010108:Oxyhemoglobins / Q000032:analysis; D011110:Polymorphism, Genetic; D014337:Trout / Q000097:blood
D006454:Hemoglobins; D010108:Oxyhemoglobins; D006433:Hemocyanins