VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Purification and properties of myeloperoxidase from mice leukocytes

   
Shafran M.G., Lyslova S.N.
PubMed Id: 3027
Year: 1975  Volume: 21  Issue: 6  Pages: 629-633
Myeloperoxidase from leucocytes of peritoneal exudate was isolated by chromatography on DEAE-Sephadex, CM-cellulose and gel filtration on Sephadex G-75. The preparation obtained was homogenous as shown by repeated gel filtration and ultracentrifugation. The enzyme was purified 302-fold, with 16% yield. The sedimentation constant was equal to 4.05 S. Molecular weight of the enzyme, determined by gel filtration on Sephadex G-100, constituted 135,000 daltons. Myeloperoxidase had two pH optima of activity--at pH 4.6 and at pH 7.6. Km for o-dianizidine was equal to 4.0-10(-3)M and for hydrogen peroxide--to 1.65-10(-4)M. Myeloperoxidase of mice leucocytes differed from the enzymes of leucocytes from other animal species in its distinctly lower sedimentation constant and thermolability.
Download PDF:
Cite as:

Shafran, M. G., Lyslova, S. N. (1975). Purification and properties of myeloperoxidase from mice leukocytes. Voprosy meditsinskoi khimii, 21(6), 629-633.
References
 1984 (vol 30)
 1983 (vol 29)
 1982 (vol 28)
 1981 (vol 27)
 1980 (vol 26)
 1979 (vol 25)
 1978 (vol 24)
 1977 (vol 23)
 1976 (vol 22)
 1975 (vol 21)
 1974 (vol 20)
 1973 (vol 19)
 1972 (vol 18)
 1971 (vol 17)
 1970 (vol 16)
 1969 (vol 15)
 1968 (vol 14)
 1967 (vol 13)
 1966 (vol 12)
 1965 (vol 11)