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. 1990 Jul 31;170(2):915-22.
doi: 10.1016/0006-291x(90)92178-3.

Isolation and characterization of a cDNA clone for a novel serine-rich neutrophil protein

P Bellavite  1 , F Bazzoni, M A Cassatella, K J Hunter, J V Bannister
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Isolation and characterization of a cDNA clone for a novel serine-rich neutrophil protein

P Bellavite et al. Biochem Biophys Res Commun. .

Abstract

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.

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