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Science 7 March 1969:
Vol. 163. no. 3871, pp. 1069 - 1071
DOI: 10.1126/science.163.3871.1069
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Articles

Cationic Protein-Bearing Granules of Polymorphonuclear Leukocytes: Separation from Enzyme-Rich Granules

H. I. Zeya 1 and J. K. Spitznagel 1

1 Department of Bacteriology and Immunology, University of North Carolina Medical School, Chapel Hill

The cationic, antibacterial proteins of polymorphonuclear leukocytes are associated with a unique subcellular particle that is separable through zonal density gradient centrifugation from acid phosphatase-containing particles as well as from particles that contain alkaline phosphatase and lysozyme. Normal macrophages, macrophages stimulated by bacillus Calmette-Guérin, and liver cells lack this particle and the associated group of cationic proteins. Particles physically and biochemically similar to slower sedimenting enzyme-rich particles of polymorphonuclear leukocytes are shared by all the tlhree cell types.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Collagenase: Localization in Polymorphonuclear Leukocyte Granules in the Rabbit.
P. B. Robertson, R. B. Ryel, R. E. Taylor, K. W. Shyu, and H. M. Fullmer (1972)
Science 177, 64-65
   Abstract »    PDF »
Myeloperoxidase: Contribution to the Microbicidal Activity of Intact Leukocytes.
S. J. Klebanoff (1970)
Science 169, 1095-1097
   Abstract »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)