Soluble and surface-bound aminopeptidase in eosinophilic blood cells from Mytilus edulis.
This study focused on soluble and surface-bound aminopeptidase (AP) in hemocytes from Mytilus edulis and on the identification of the enzyme-producing blood cells. The cell extract hydrolyzed alanine p-nitroanilide (Ala-pNA) with an optimum between pH 6.4 and 7.0. Following native gradient PAGE of extract, alanyl methoxy-naphthylamide (AMNA) was converted by one band with an estimated molecular weight of 375kDa; it included at least ten putative AP-isozymes with isoelectric points between pH 4.5 and 5.8. In addition to this soluble form, electron microscopy revealed simultaneous conversion of AMNA on the surface of blood cells. Individual mussels expressed AP-molecules in 23-39% of their hemocytes. These cells were shown to represent eosinophilic granulocytes.
Renwrantz
Lothar
L
Biozentrum Grindel und Zoologisches Museum, Martin-Luther-King-Platz 3, Hamburg, Germany. L.Renwrantz@gmx.de
Lam
Anna
A
D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D006434:Hemocytes / Q000201:enzymology* / Q000648:ultrastructure; D007527:Isoenzymes / Q000378:metabolism; D049880:Mytilus edulis / Q000201:enzymology*
D007527:Isoenzymes; D000626:Aminopeptidases