Abstract
The subunit composition of Panulirus interruptus hemocyanin has been studied. Equilibrium sedimentation, gel chromatography and sodium dodecyl sulphate-polyacrylamide electrophoresis reveal a hexameric structure for this hemocyanin, with a molecular weight of 450,000 for the undissociated protein and 75,000 for the subunits. Amino acid analysis data suggest homogeneity of the polypeptide chain. X-ray diffraction gives the cell parameters a = 119·8, b = 193·1 and c = 122·2 , β = 118·1o. The asymmetric unit contains one molecule. Oxygen binding data show the undissociated protein to be co-operative while the dissociated protein binds oxygen non-co-operatively with a low oxygen affinity compared to that of whole molecules.
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