PMID: 7528540Dec 15, 1994Paper

Isolation and characterization of circulating complex between human pregnancy-associated plasma protein-A and proform of eosinophil major basic protein

Biochimica Et Biophysica Acta
Claus OxvigLars Sottrup-Jensen

Abstract

The plasma protein previously known as pregnancy associated plasma protein-A (PAPP-A) and believed to contain only one kind of polypeptide chain has recently been shown to be a complex containing two different chains in equimolar amounts. One of the chains is now defined as the PAPP-A subunit, and the other has been identified as the proform of eosinophil major basic protein (proMBP) (Oxvig et al. (1993) J. Biol. Chem. 268, 12243-12246). A procedure for large scale preparation of the circulating complex (PAPP-A/proMBP) from pooled pregnancy serum is described. The amino acid and carbohydrate compositions of the isolated reduced and carboxymethylated PAPP-A (199 kDa) and proMBP subunits (38 kDa), and of the intact PAPP-A/proMBP have been determined. The PAPP-A and proMBP subunits contain 13.4% (w/w) and 38.6% (w/w) carbohydrate, respectively, and the intact complex contains 17.4% (w/w) carbohydrate. The PAPP-A subunit contains N-bound carbohydrate groups. In contrast, the proMBP subunit contains both N- and O-bound groups as well as glycosaminoglycan, previously found among plasma proteins only in inter-alpha-trypsin inhibitor and pre-alpha-trypsin inhibitor. It is shown that PAPP-A/proMBP can competitively inhibit human leucocy...Continue Reading

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Citations

Jul 19, 2005·Journal of Assisted Reproduction and Genetics·Dorothea M WunderNick A Bersinger
Oct 29, 1996·Clinica Chimica Acta; International Journal of Clinical Chemistry·Q P QinB Nørgaard-Pedersen
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Mar 17, 2016·Atherosclerosis·Lasse B SteffensenClaus Oxvig
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Apr 25, 2008·The Journal of Biological Chemistry·Jakob H MikkelsenClaus Oxvig

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