8. Vol. 170, N3. P. 351—365.

О seas R. S., Allen J., Yang H. H. et al. Rabbit cationic protein enhances leukocyte adhesiveness II Immunology. 1981a. Vol.33. P.523—526.

Oseas R. S., Yang H. H., Baehner R. L., Boxer L A. Lactoferrin: a promoter of polymorphonuclear leukocyte adhesiveness В Blood. 1981b. Vol.57. P.939—945.

Osserman E. F., Canfield E, Bagchok S. Lysozyme. New York; London, 7974.

Ouellette A. J., Lualdi J. C. A novel mouse gene family coding for cationic, cyste-in-rich peptides // J. Biol. Chem. 7990. Vol.265, N17. P.9831—9837.

Ouellette A. J., Greco R. M., James M. et al. Development regulation of cryptdin, a corticostatin/defensin precursor in RNA in mouse small intestinal cryptepithelium В J. Cell Biol. 7959a. Vol. 108. P. 1687—1695.

Ouellette A. J., Prautcheva D., Ruddle F. H, James M. Localization of the cryptdin locus on mouse chromosome 8 В Genomics. 1989b. Vol. 5. P. 233—239.

Ouellette A. J., Miller S. I., Henschen A. #., Selsted M. E. Purification and primary structure of murine cryptdin-1, a Paneth cell defensin В FEBS Lett. 7992. Vol. 304, N2. P. 146—148.

Ouellette A. J., Hsieh M. M., Nosek M. T. et al. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms В Infect, and Immun.

7994. Vol.62. P.5040—5047.

Owen C.A., Campbell M.A., Sannes P.L et al. Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases В J. Cell. Biol. 7995. Vol.131. P.775—789.

Palfree R. G„ Sadro L, Solomon S. The gene encoding the human corticostatin HP-4 precursor contains a recent 86-base duplication and is located on chromosome 8 В Mol. Endocrin. 1993. Vol.7, N2. P. 199—205.

Panyim S., Chalkley R. High resolution acrilamyde gel electrophoresis of histones В Arch. Biochem. and Biophys. 7969. Vol. 130, N2. P. 337—346.

Panyutich A. V., Ganz T. Activated alpha 2-Macroglobulin is a principal defensin-binding protein В Amer. J. Respirat. Cell and Molec. Biol. 7997. N5. P. 101—106.

Panyutich A. V., Voitenok N. N.. Lehrer R. I., Ganz T. An enzyme immunoassay for human defensins В J. Immunol. Meth. 7997. Vol. 141. P. 149—155.

Panyutich A. V., Baturevich E. A., Kolesnikova T. S., Ganz T. The effect of biotinylati-on on the antigenic specificity of anti-defensin monoclonal antibodies В J. Immunol. Meth. 1993a, Vol. 158. P. 237—242.

Panyutich A. V., Panyutich E.A., Krapivin V.A. et al. Plasma defensin concentrations are elevated in patients with septicemia or bacterial meningitis В J. Lab. and Clin. Med. 1993b. Vol. 122, N2. P. 202—207.

Panyutich A. V., Szold О., Poon P. H. et al. Identification of defensin binding to CI complement В FEBS Lett. 1994. Vol. 356. P. 169—173.

Panyutich A. V., Hiemstra P. S., Van Wetering S., Ganz T. Human neutrophil defensin and serpins form complexes and inactivate each other В Amer. J. Respirat. Cell and Molec. Biol. 7995. Vol. 12. P. 351—357.

Pardi A., Hare D., Selsted M. E. et al. Solution structures of the rabbit neutrophil defensin NP-5 В J. Mol. Biol. 1988. Vol.201, N3. P.625—636.

Parra-Lopez C, Baer Af. Т., Groisman E. A. Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium В EMBO J.

7995. Vol. 12. P. 4053—4062.

Parry Af. F., Root Я К., Metcalf J. A. et al. Myeloperoxidase deficiency: Prevalence and clinical significance # Amer. Int. Med. 1981. Vol.95, N3. P.293—301.

Patterson-Delafield J., Martinez Я J., Lehrer R. J. Microbocidal cationic prolan* in rabbit alveolar macrophages: a potential host defense mechanism В Infect, and (мент. 7950. Vol. 30. P. 180—192. Patterson-Delafield J., Szklarek D., Martinez R., Lehrer j?. J. Microbicidal cationic proteins of rabbit alveolar macrophages: amino acid composition and functional attributes / Infect, and Immun. 1981. Vol.31, N2. P.723—731.

Penniall R., Spitznagel J. K. Chicken neutrophils: oxidative metabolism in phagocytic cells devoid of myeloperoxidase / Proc. Nat. Acad. Sci. USA. 1975. Vol.72. P.5012— 5015.

Penniall R., Holbrook J. P., Zeya H. I. The inhibition of cytochrome oxidase by lysosomal cationic proteins of rabbit polymorphonuclear leukocytes # Biochem. and Biophys. Res. Communs. 1972. Vol.47. P. 1270.

Peppin G.J., Weiss S.J. Activation of endogenous metalloproteinase, gelatinase, by triggered human neutrophils 0 Proc. Nat. Acad. Sci. USA. 1986. Vol.83. P.4322— 4326.

Pereira H. A. CAP37, a neutropbil-derived multifunctional inflammatory mediator 0 J. Leukocyte. Biol. 1995. Vol.57. P.805—812.

Pereira H. A., Martin L. E., Spitznagel J. K. Quantitation of a cationic antimicrobial granule protein of human polymorphonuclear leukocytes by ELISA0 J. Immunol. Meth. 1989. Vol. 117, N1. P. 115—120.

Pereira H. A., Shaftr W. M., Pohl J. et al. CAP37, a human neutrophil derived chemotactic factor with monocyte specific activity 0 J. Clin. Invest. 1990a. Vol.85, N4. P. 1468—1476.

Pereira H. A., Spitznagel J. K., Pohl J. et al CAP37, a 37 kDa human neutrophil granule cationic protein shares homology with inflammatory proteinases # Life Sci. 1990b. Vol.46, N3. P. 189—196.

Pereira H. A., Spitznagel J. K„ Winton E. F. et al. The ontogeny of a 57 kDa cationic antimicrobial protein of human polymorphonuclear leukocytes: localization to a novel granule population 0 Blood. 1990c. Vol.76. P.825—834.

Pereira H. A., Erdem I.. Pohl J., Spitznagel J. K. Synthetic bactericidal peptide based on CAP37 — a 37 kDa human neutrophil granule-associated cationic antimicrobial protein chemotactic for monocytes 0 Proc. Nat. Acad. Sci. USA. 1993. Vol.90. P. 4733—4737.

Peters C. W„ Kruse U., Pollwein R. et al. The human lysozyme gene-sequence organization and chromosomal localization # Eur. J. Biochem. 1989. Vol.182, N3. P.507—516.

Peters M. S., Rodrigues M., Gleich G. J. Localization o