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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Isolation and characterization of a cDNA clone for a novel serine-rich neutrophil protein. Bellavite, P., Bazzoni, F., Cassatella, M.A., Hunter, K.J., Bannister, J.V. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
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