Ontology highlight
ABSTRACT:
SUBMITTER: Ten RM
PROVIDER: S-EPMC2189302 | biostudies-other | 1989 May
REPOSITORIES: biostudies-other
Ten R M RM Pease L R LR McKean D J DJ Bell M P MP Gleich G J GJ
The Journal of experimental medicine 19890501 5
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 corr ...[more]