Open AccessHigh Phospholipase Activities in Amoebae of Dictyostelium discoideum
Author(s) -
Ferber Ernst,
Munder Paul G.,
Fischer Herbert,
Gerisch Günther
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb00284.x
Subject(s) - lysophospholipase , dictyostelium discoideum , dictyostelium , phospholipase , biochemistry , proteases , biology , phospholipase a , digitonin , chemistry , enzyme , microbiology and biotechnology , phospholipase a2 , gene
Amoebae of the cellular slime mold Dictyostelium discoideum exhibit high activities of particlebound phospholipase A and lysophospholipase. The activity of phospholipase A in homogenates of Dictyostelium cells was found to be 3,8 nmoles × mg protein −1 × min −1 and of lysophospholipase 186 nmoles × mg protein −1 × min −1 . p ‐Chloromercuribenzoate ( p CMB) and digitonin were found to be inhibitors of phospholipase A while these compounds did not influence the activity of the lysophospholipase. There was no indication that homogenates of Dictyostelium contain phospholipase C activity. The lysolecithin‐acylating activity could only be detected in cell suspensions which were diluted before homogenisation to 2 mg protein/ml (2 × 10 7 cells/ml) probably because of the action of proteases or phospholipases in more concentrated homogenates. The results are discussed in view of the membrane activies of Dictyostelium amoebae during various morphogenetic stages.