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Haemocyanin of some Oniscidea
Acta Biochimica Polonica
|January 1, 1991
Summary
Oniscidea haemocyanin primarily exists as a 16S hexamer in their hemolymph. Its alkaline dissociation is influenced by pH and divalent cations, with specific amino acid compositions noted.
Area of Science:
- Biochemistry
- Marine Biology
- Crustacean Physiology
Background:
- Haemocyanins are copper-containing respiratory proteins found in many arthropods and mollusks.
- Oniscidea (woodlice) possess haemocyanin in their hemolymph for oxygen transport.
- Understanding haemocyanin structure and function is crucial for invertebrate physiology.
Purpose of the Study:
- To characterize the quaternary structure of Oniscidea haemocyanin.
- To investigate the factors affecting the alkaline dissociation of the 16S haemocyanin component.
- To determine the amino acid composition of the 16S haemocyanin.
Main Methods:
- Ultracentrifugation to determine haemocyanin component sizes (16S, 5S, 24S).
- pH-dependent and cation-dependent dissociation studies.
- Amino acid analysis of the 16S haemocyanin component.
Main Results:
- Oniscidea haemocyanin is predominantly a 16S hexamer (90%), with minor 5S and 24S components.
- Alkaline dissociation of 16S haemocyanin is sensitive to pH and the presence of Ca2+ and Mg2+.
- The 16S component contains 23-24.5% acidic amino acids, 15-18% basic amino acids, and low levels of tryptophan and cysteine.
Conclusions:
- The 16S hexamer is the primary functional form of haemocyanin in Oniscidea.
- Environmental factors like pH and divalent cations play a role in regulating haemocyanin dissociation and potentially oxygen-binding.
- The amino acid profile of the 16S component provides insights into its structural stability and functional properties.