Back to Search Start Over

Human erythrocyte pyrimidine 5′-nucleotidase, PN-I, is identical to p36, a protein associated to lupus inclusion formation in response to α-interferon

Authors :
Franca Saccucci
Adolfo Amici
Silverio Ruggieri
Nadia Raffaelli
Monica Emanuelli
Giulio Magni
Source :
Scopus-Elsevier
Publication Year :
2000
Publisher :
American Society of Hematology, 2000.

Abstract

Erythrocyte maturation is accompanied by RNA degradation and release of mononucleotides. We have previously purified PN-I, a pyrimidine nucleotidase whose deficiency is associated with hemolytic anemia. Computer-aided analysis of PN-I tryptic and CNBr peptide sequences revealed substantial identity with tryptic peptide sequences reported for p36, an α-interferon-induced protein. PN-I partial sequences were matched through the expressed sequence tag database with different human complementary DNA (cDNA) clones, whose sequences were exploited to screen a human placenta cDNA library. PN-I cDNA, coding for a 286-residue protein, was expressed in Escherichia coli, yielding a fully active recombinant enzyme. The recombinant protein sequence comprised the peptide sequences determined for PN-I and p36. Rabbit antisera raised against two peptides deriving from p36 and PN-I tryptic digestions, respectively, recognized both wild-type and recombinant PN-I. Molecular properties of the two proteins were essentially the same. We conclude that p36 and PN-I are identical proteins.

Details

ISSN :
15280020 and 00064971
Volume :
96
Database :
OpenAIRE
Journal :
Blood
Accession number :
edsair.doi.dedup.....2707d7c0008f87083cb961cda291171f
Full Text :
https://doi.org/10.1182/blood.v96.4.1596.h8001596_1596_1598