Zoeken
Zoeken kan via de modus 'eenvoudig zoeken' (één veld) of uitgebreid via 'geavanceerd zoeken' (meerdere velden). Zo kan je bv. zoeken op een combinatie van een auteursnaam (auteur), een jaartal (jaar) en een documenttype.
Boekenmand
Nuttige resultaten kan je aanvinken en toevoegen aan een mandje. De inhoud hiervan kan je exporteren of afdrukken (naar bv. PDF).
RSS
Op de hoogte blijven van nieuw toegevoegde publicaties binnen uw interessegebied? Dit kan door een RSS-feed (?) te maken van jouw zoekopdracht.
nieuwe zoekopdracht
Salinity related physiological and genetic differences between populations of Mytilus edulis
In: Biological Journal of the Linnean Society. Academic Press: London; New York. ISSN 0024-4066; e-ISSN 1095-8312
|  |
| Trefwoorden |
Biology > Physiology
Genetics
Populations
Properties > Chemical properties > Salinity
Variations
Mytilus edulis Linnaeus, 1758 [WoRMS]
Marien/Kust |
| Auteurs | | Top |
- Koehn, R.K.
- Bayne, B.L.
- Moore, M.N.
- Siebenaller, J.F.
|
|
|
| Abstract |
Aminopeptidase-I, the enzymatic product of the Lap locus, liberates N-terminal neutral and aromatic amino acids from oligopeptides. The enzyme is associated with the brush border of the intestine and the extensive lysosomal system in the digestive tubule cells; the enzyme functions in oligopeptide degradation and possibly amino acid transport. The Lap locus is genetically polymorphic and allele frequencies differ between populations according to environmental salinities.Using cell-free lysosomes, we show salinity related differences in both lysosomal membrane latency and lysosomal and cytosolic free-amino acid concentrations. Differences in the response of the lysosomal aminopeptidase-I enzyme to differences or changes in salinity are discussed.Antibodies against aminopeptidase-I enzyme were used to demonstrate that alleles of the Lap locus exhibit different specific activities per unit enzyme concentration. In oceanic populations, the concentrations of aminopeptidase-I enzyme of individual phenorypes are equal, suggesting that variation of specific activity among phenorypes is due to allele specific differences in catalytic efficiency. In estuarine populations, total enzyme activity is lower, which is partially due to a significantly lower concentration of aminopeptidase-I enzyme of one homozygote genotype.The consequences of a change in environmental salinity can be measured on the biochemical, physiological, and population genetic levels. We discuss the possible mechanisms by which salinity variations are responsible for the genetic polymorphism of aminopeptidase-I. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
