|Leucine Aminopeptidase (Aminopeptidase-I), N-Acetyl-Beta-Hexosaminidase and lysosomes in the mussel, Mytilus edulis L. in response to salinity changes|
Moore, M.N.; Koehn, R.K.; Bayne, B.L. (1980). Leucine Aminopeptidase (Aminopeptidase-I), N-Acetyl-Beta-Hexosaminidase and lysosomes in the mussel, Mytilus edulis L. in response to salinity changes. J. Exp. Zool. 214: 239-249
In: The Journal of Experimental Zoology. Wiley Interscience: New York, etc.. ISSN 0022-104X, more
Osmoregulation; Salinity effects; Bivalvia [WoRMS]; Marine
|Authors|| || Top |
- Moore, M.N.
- Koehn, R.K.
- Bayne, B.L.
The intracellular distribution of aminopeptidase-I in the intestinal and digestive cells of Mytilus edulis has been shown to be the same as the lysosomal marker enzymes beta-glucuronidase and N-acetyl-beta-hexosaminidase. Activity for these enzymes was also associated with the intestinal apical cytoplasm and microvillous border where there was pronounced staining for aminopeptidase-I. Experimental alterations of salinity induced changes in both microdensitometrically and spectrophotometrically determined aminopeptidase-I activity, as an increase with raised salinity and a decrease with lowered salinity. Lysosomal hexosaminidase showed similar changes in activity with altered salinity. Cytochemically determined lysosomal stability was also responsive to salinity changes, indicative of alterations in lysosomal functional capability. The lysosomal distribution of aminopeptidase-I is discussed in terms of the function of lysosomes in intracellular protein turnover, their high concentrations of free amino acids, and the possible roles which these might play in intracellular osmoregulation in response to salinity change.