Tubular polymers derived from Helix pomatia beta-hemocyanin.
Upon trypsinolysis Helix pomatia beta-hemocyanin forms long tubular structures, which appear to be linear polymers of hemocyanin molecules from which the collar structure has been removed. Polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate shows that only few peptide bonds are hydrolyzed by trypsin. The structure of the polymers has been investigated by electron microscopy, combined with optical diffraction. Preliminary X-ray diffraction data are presented. Functional properties of the polymers are similar to those of the native protein. Both show a calciumion-dependent co-operativity of oxygen binding and a Bohr effect. The results suggest that the collar of a hemocyanin molecule has no special function in the process of (co-operative) oxygen binding, different from that of the wall of the molecule.
D000818:Animals; D001665:Binding Sites; D006372:Helix, Snails; D006433:Hemocyanins; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D010100:Oxygen; D011485:Protein Binding; D011487:Protein Conformation; D014357:Trypsin; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D006433:Hemocyanins; D014357:Trypsin; D010100:Oxygen