Isolation and characterization of a cDNA clone for a novel serine-rich neutrophil protein.
A cDNA expression library from pig blood neutrophils was immunoscreened with a rabbit antiserum raised against a 32 kDa neutrophil membrane phosphoprotein. Previous work indicated this protein as a component of the superoxide-forming NADPH oxidase enzyme complex (1,2). Only one cDNA clone (B+) was highly positive. The B+ clone contained a 1109 bp insert, with an open reading frame encoding for 284 amino acids. The deduced B+ amino acid sequence contained a 72 amino acid domain with proline and glutamine repeats and two domains extremely enriched with serine residues. The isolated cDNA hybridizes with a 3.1 kb mRNA expressed in pig and human leukocytes.
Institute of General Pathology, University of Verona, Italy.
P
P
Bellavite
F
F
Bazzoni
M A
MA
Cassatella
K J
KJ
Hunter
J V
JV
Bannister
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001798:Blood Proteins / Q000235:genetics*; D015152:Blotting, Northern; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000378:metabolism*; D010750:Phosphoproteins / Q000096:biosynthesis / Q000235:genetics*; D012313:RNA / Q000032:analysis; D011817:Rabbits; D012694:Serine / Q000235:genetics; D013552:Swine
D001798:Blood Proteins; D008565:Membrane Proteins; D010750:Phosphoproteins; C065182:neutrophil membrane protein gp32; D012694:Serine; D012313:RNA; D004247:DNA