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Updated: Aug 16, 2026

Laboratory Protocol for Genetic Gut Content Analyses of Aquatic Macroinvertebrates Using Group-specific rDNA Primers
Published on: October 5, 2017
Biochemical and molecular characterisation of hemocyanin from the amphipod Gammarus roeseli: complex pattern of
Silke Hagner-Holler1, Kristina Kusche, Anne Hembach
1Institute of Zoology, University of Mainz, Müllerweg 6, 55099 Mainz, Germany. burmeste@uni-mainz.de
Abstract:
Hemocyanin is a copper-containing respiratory protein that is widespread within the arthropod phylum. Among the Crustacea, hemocyanins are apparently restricted to the Malacostraca. While well-studied in Decapoda, no hemocyanin sequence has been known from the 'lower' Malacostraca. The hemocyanin of the amphipod Gammarus roeseli is a hexamer that consists of at least five distinct subunits. The complete cDNA sequence of one subunit and a tentative partial sequence of another subunit have been determined. The complete G. roeseli hemocyanin subunit comprises 2,150 bp, which translates in a protein of 672 amino acids with a molecular mass of 76.3 kDa. Phylogenetic analyses show that, in contrast to previous assumptions, the amphipod hemocyanins do not belong to the alpha-type of crustacean hemocyanin subunits. Rather, amphipod hemocyanins split from the clade leading to alpha and gamma-subunits most likely at the time of separation of peracarid and eucarid Crustacea about 300 million years ago. Molecular clock analyses further suggest that the divergence of beta-type subunits and other crustacean hemocyanins occurred around 315 million years ago (MYA) in the malacostracan stemline, while alpha- and gamma-type subunits separated 258 MYA, and pseudohemocyanins and gamma-subunits 210 million years ago.
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