Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family.
Human eosinophil peroxidase (EPO) was purified from eosinophil granules derived from the peripheral blood of patients with eosinophilia. The molecular mass of the H and L subunits was determined by gel filtration to be 57,000 and 11,000 daltons, respectively. The partial amino acid sequences of both subunits were used to construct oligonucleotides for the screening of several cDNA libraries, including one derived from human-induced umbilical cord mononuclear cells. A cDNA clone was isolated corresponding to EPO. The nucleotide sequence revealed an open reading frame of 2,106 bp, corresponding to a prosequence, L chain, and H chain, in this order. Comparison of the EPO nucleotide sequence with other peroxidases, such as myeloperoxidase, suggests the existence of a multigene family.
Ten
R M
RM
Department of Immunology, Mayo Clinic, Rochester, Minnesota 55905.
Pease
L R
LR
McKean
D J
DJ
Bell
M P
MP
Gleich
G J
GJ
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D002478:Cells, Cultured; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D004804:Eosinophils / Q000201:enzymology*; D005312:Fetal Blood / Q000166:cytology; D006801:Humans; D007963:Leukocytes, Mononuclear / Q000201:enzymology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D005810:Multigene Family; D009693:Nucleic Acid Hybridization; D009195:Peroxidase / Q000235:genetics* / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid
D004247:DNA; D009195:Peroxidase