Granule enzymes of polymorphonuclear neutrophils: A phylogenetic comparison.
The functional significance of granule enzymes in polymorphonuclear leukocytes (PMN) is not fully understood because of the multiplicity of the enzymes and the rare occurrence of deficiencies in man. In order to select appropriate laboratory animals for functional studies, a phylogenetic comparison of enzyme levels in animal and human PMN was undertaken. Neutrophils were obtained from a variety of laboratory animals and man; the activities of alkaline phosphatase, lysozyme, myeloperoxidase, and beta-glucuronidase were determined by histochemical and analytical techniques. Marked interspecies differences in enzyme activity were found; many species were deficient in alkaline phosphatase or lysozyme. Differences in pH optima and metal requirements of alkaline phosphatase were not of sufficient magnitude to explain the variations of this enzyme.
D000469:Alkaline Phosphatase / Q000097:blood; D000818:Animals; D002415:Cats; D002417:Cattle; D002645:Chickens; D006224:Cricetinae; D003594:Cytoplasmic Granules / Q000201:enzymology*; D004285:Dogs; D005777:Geese; D005966:Glucuronidase / Q000097:blood; D006041:Goats; D006168:Guinea Pigs; D000882:Haplorhini; D006736:Horses; D006801:Humans; D051379:Mice; D009113:Muramidase / Q000097:blood; D009504:Neutrophils / Q000201:enzymology*; D009195:Peroxidase / Q000097:blood; D010802:Phylogeny; D011817:Rabbits; D051381:Rats; D012756:Sheep; D013045:Species Specificity
D009195:Peroxidase; D000469:Alkaline Phosphatase; D009113:Muramidase; D005966:Glucuronidase