Structural Basis for Salinity‐Induced Alteration in Oxygen Binding by Haemocyanin from the Estuarine Amphipod Chaetogammarus marinus (L.)

Abstract In the estuarine amphipod Chaetogammarus marinus, differences in O2 binding by haemocyanins (Hc) could be related to natural and salinity‐related quantitative variation in just one polypeptide subunit (band 2) and not to variations in any of the other seven bands present. Band 2 was always present, irrespective of salinity treatment, and naturally makes up 6%–36% of the total Hc. However, low salinity exposure ( \documentclass{aastex} \usepackage{amsbsy} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{bm} \usepackage{mathrsfs} \usepackage{pifont} \usepackage{stmaryrd} \usepackage{textcomp} \usepackage{portland,xspace} \usepackage{amsmath,amsxtra} \usepackage[OT2,OT1]{fontenc} \newcommand\cyr{ \renewcommand\rmdefault{wncyr} \renewcommand\sfdefault{wncyss} \renewcommand\encodingdefault{OT2} \normalfont \selectfont} \DeclareTextFontCommand{\textcyr}{\cyr} \pagestyle{empty} \DeclareMathSizes{10}{9}{7}{6} \begin{document} \landscape $S=4$ \end{document} ‰ for 48–49 h, \documentclass{aastex} \us...