Hemocyanins of Muricidae: New 'Insights' Unravel an Additional Highly Hydrophilic 800 kDa Mass Within the Molecule.

ABSTRACT: Hemocyanins are giant oxygen transport proteins that freely float within the hemolymph of most molluscs. The basic quaternary structure of molluscan hemocyanins is a cylindrical decamer with a diameter of 35 nm which is built of 400 kDa subunits. Previously published results, however, showed that one out of two hemocyanin subunits of Rapana venosa encompasses two polypeptides, one 300 kDa and one 100 kDa polypeptide which aggregate to typical 4 MDa and 8 MDa hemocyanin (di-)decamer molecules. It was shown that the polypeptides are bound most probably by one or more cysteine disulfide bridges but it remained open if these polypeptides were coded by one or two genes. Our here presented results clearly showed that both polypeptides are coded by one gene only and that this phenomenon can also

SUBMITTER: Schafer GG 

PROVIDER: S-EPMC7884596 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature