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O Sand
Aarhus University
Molecular biologyPeptide sequenceBiochemistryMajor basic proteinBiology
6Publications
6H-index
757Citations
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Publications 6
Newest
#1Claus Oxvig (AU: Aarhus University)H-Index: 45
#2O Sand (AU: Aarhus University)H-Index: 6
Last. Lars Sottrup-Jensen (AU: Aarhus University)H-Index: 51
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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 submit, 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 cir...
96 CitationsSource
#2Claus OxvigH-Index: 45
Last. Lars Sottrup-JensenH-Index: 51
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The amino acid sequence of human pregnancy-associated plasma protein-A (PAPP-A), a component of the circulating complex with the proform of eosinophil major basic protein (proMBP), has been determined from partial protein sequencing and from sequencing of cloned cDNA. The PAPP-A monomer contains 1547 amino acid residues, but is derived from a larger precursor of placental origin. PAPP-A contains 82 Cys residues, which are all bridged, 14 putative sites for N-glycosylation, and 7 putative sites f...
74 CitationsSource
#1Claus Oxvig (AU: Aarhus University)H-Index: 30
#2O Sand (AU: Aarhus University)H-Index: 6
Last. Lars Sottrup-Jensen (AU: Aarhus University)H-Index: 51
view all 5 authors...
Abstract A previously unrecognized association between pregnancy-associated plasma protein-A (PAPP-A) and the proform of eosinophil major basic protein (proMBP) is demonstrated. PAPP-A isolated from pooled pregnancy serum is shown to be a disulfide-bridged complex with proMBP (PAPP-A/proMBP) in which the subunits of the constituents are present in a 1:1 molar ratio. The results are the outcome of analysis of tryptic and CNBr/tryptic peptides from PAPP-A/proMBP, sequence analysis of intact and re...
151 Citations
#1Torsten Nygaard Kristensen (AU: Aarhus University)H-Index: 40
#2Søren K. Moestrup (AU: Aarhus University)H-Index: 72
Last. Lars Sottrup-Jensen (AU: Aarhus University)H-Index: 51
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The human placental receptor (α2MR) for α2-macroglobulin-proteinase complexes contains 3 polypeptides of approx. 500 kDa, 85 kDa, and 40 kDa. N-terminal sequence analysis of the 500 kDa and 85 kDa polypeptides, analysis of a random selection of peptides covering 536 residues from these polypeptides, and analysis of a 1772 bp cDNA encoding part of the 500 kDa polypeptide provide evidence that the 500 kDa and 85 kDa chains are the α- and β-subunits, respectively, of a recently cloned hepatic membr...
260 CitationsSource
#1Lars Sottrup-JensenH-Index: 51
#2O SandH-Index: 6
Last. G H FeyH-Index: 1
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Abstract The amino acid sequence of a 90-residue segment of human pregnancy zone protein containing its bait region has been determined. Human alpha 2-macroglobulin, human pregnancy zone protein, and rat alpha 1-macroglobulin, alpha 2-macroglobulin, and alpha 1-inhibitor 3 variants 1 and 2 constitute a group of homologous proteins; but the sequences of their bait regions are not related, and they differ in length (32-53 residues). The alpha-macroglobulin bait region is located equivalently with ...
153 Citations
#2E EjlersenH-Index: 1
Last. Lars Sottrup-JensenH-Index: 51
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Lymphokine activated killer cell lysis of K562 cells was inhibited by alpha 2-macroglobulin (alpha 2M), soybean trypsin inhibitor, and alpha 1-proteinase inhibitor. In serum free medium 2 mg/ml alpha 2M suppressed target cell lysis in a 4-h cytotoxic assay with about 40%. Suppression was dose and time dependent. Cytotoxicity was unaffected by alpha 2M concentrations less than 0.25 mg/ml, and by alpha 2M added later than 1.5 h from start of assay. Pre-treatment of effector (but not of target) cel...
23 Citations
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