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. 1977 Dec 1;167(3):839-41.
doi: 10.1042/bj1670839.

Phospholipase A activity associated with membranes of human polymorphonuclear leucocytes

R Franson, J Weiss, L Martin, J K Spitznagel, P Elsbach

Phospholipase A activity associated with membranes of human polymorphonuclear leucocytes

R Franson et al. Biochem J. .

Abstract

Homogenates of human polymorphonuclear leucocytes (granulocytes) contain a Ca2+-dependent phospholipase A with optimal activity pH7.0. This enzyme is membrane-bound and is enriched in crude cytoplasmic-granule fraction. Ratezonal centrifugation of the cytoplasmic-granule fraction demonstrates that the phospholipase A is associated not only with specific- and azurophilic-granule populations but also with an 'empty' vesicular fraction containing 85% of the total alkaline phosphatase activity of whole homogenate. Thus this phospholipase is associated with granule as well as with other cellular membranes of human granulocytes.

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