Soluble and surface-bound aminopeptidase in eosinophilic blood cells from Mytilus edulis.
J Invertebr Pathol
; 103(1): 68-70, 2010 Jan.
Article
in En
| MEDLINE
| ID: mdl-19822151
ABSTRACT
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Mytilus edulis
/
Aminopeptidases
/
Hemocytes
Limits:
Animals
Language:
En
Journal:
J Invertebr Pathol
Year:
2010
Document type:
Article
Affiliation country: