A Possible Role Of Alpha-Amylase Isoenzymes From The Style Of The Mussel Choromytilus-Meridionalis (Krauss) Following Thermal-Acclimation

Newell, RC, Parker, I and Cook, PA 1980 A Possible Role Of Alpha-Amylase Isoenzymes From The Style Of The Mussel Choromytilus-Meridionalis (Krauss) Following Thermal-Acclimation. Journal of Experimental Marine Biology and Ecology, 47 (1). 01-Aug. https://doi.org/10.1016/0022-0981(80)90133-1

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Abstract/Summary

Separation of the proteins comprising the crystalline style of the mussel Choromytilus meridionalis (Krauss) by anion exchange chromatography shows that there are three fractions displaying α-amylase activity in both warm- and cold-acclimated mussels. These fractions correspond with one or more proteins which remain unbound to the resin (Peak I), a bound fraction which is eluted at 100–150 mM NaCl (Peak II) and a further fraction which is eluted at 200–250 mM NaCl (Peak III) but which may represent contamination carried over from Peak II. Cold-acclimation to 8°C results in the appearance of a fourth α-amylase fraction (Peak IV) which is eluted from the column between 300–400 mM NaCl. Thermal acclimation also results in changes in the activities of Fractions I–IV such that a specific activity of 0.47 mg glucose liberated per A280 unit of protein per 8 min incubation at 8°C in Fraction IV is increased nearly 10-fold to a specific rate of 4.10 in protein Fraction I following acclimation to 22°C. It is suggested that an increased of digestive activity may be of equal importance to a suppression of metabolic costs in the maintenance of energy flow into growth and reproduction in ectothermic organisms which experience an increase of environmental temperature, especially in bivalves such as C. meridionalis which do not show a compensatory increase in filtration rate.

Item Type:	Publication - Article
Subjects:	Ecology and Environment Marine Sciences
Divisions:	Plymouth Marine Laboratory > Other (PML)
Depositing User:	EPrints Services
Date made live:	11 Feb 2014 15:54
Last Modified:	06 Jun 2017 16:03
URI:	https://plymsea.ac.uk/id/eprint/2787

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