PMID: 1204634Dec 1, 1975Paper

Tubular polymers derived from Helix pomatia beta-hemocyanin

European Journal of Biochemistry
J F Van BreemenE F van Bruggen

Abstract

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.

Citations

Jan 1, 1983·Progress in Biophysics and Molecular Biology·H D EllertonH A Robinson
Jan 1, 1988·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·N B TerwilligerM P Morse
Jan 1, 1991·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·T T Herskovits, M G Hamilton
Jul 28, 2001·Micron : the International Research and Review Journal for Microscopy·K IdakievaS Stoeva
Oct 1, 1979·European Journal of Biochemistry·J F Van BreemenE F Van Bruggen
Feb 1, 1997·Micron : the International Research and Review Journal for Microscopy·J R HarrisJ Markl
Feb 1, 1982·Quarterly Reviews of Biophysics·K E van Holde, K I Miller
Dec 5, 1990·Journal of Molecular Biology·N BoissetJ Frank
Jan 1, 1980·Ultramicroscopy·W TichelaarE F van Bruggen

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