The effect of enzyme digestions on the activity of eosinophil chemotactic factor of anaphylaxis (EFC-A).
Preparations of ECF-A derived from anaphylactic guinea-pig lung diffusates were subjected to a variety of enzymatic degradations.  The enzymes employed had specificityonly for their appropiate subtstates.  No effect was found following treatmentwith relatively high doses of trypsin, alpha-chymotrypsin, pronase, alkaline phosphataseand sialidase.  In contrast a loss of activity was demonstated in a dose-dependent fashion following incubation with tyrosinase, aryl sulphatase and leucine aminopeptidase, suggesting that ECF-A contains a phenolic hydroxyl group, a sulphate ester anda peptide linkage with a free alpha-amino group.
D000469:Alkaline Phosphatase; D000707:Anaphylaxis; D000818:Animals; D004156:Catechol Oxidase; D002633:Chemotaxis; D002918:Chymotrypsin; D004305:Dose-Response Relationship, Drug; D004804:Eosinophils / Q000276:immunology*; D006168:Guinea Pigs; D007931:Leucyl Aminopeptidase; D008168:Lung / Q000201:enzymology; D009439:Neuraminidase; D010455:Peptides / Q000032:analysis; D010636:Phenols / Q000032:analysis; D011402:Pronase; D013429:Sulfatases; D013431:Sulfates / Q000032:analysis; D014357:Trypsin
D010455:Peptides; D010636:Phenols; D013431:Sulfates; D004156:Catechol Oxidase; D000469:Alkaline Phosphatase; D013429:Sulfatases; D009439:Neuraminidase; D007931:Leucyl Aminopeptidase; D002918:Chymotrypsin; D014357:Trypsin; D011402:Pronase