Purification and characterization of six annexins from human placenta.
Isolation of six calcium-binding proteins from human placenta is described by means of hydrophobic chromatography, calcium-dependent adsorption to heparin-Sepharose and ion-exchange chromatography. These proteins were characterized and identified as PP4, PP4-X, PAP III, p68 and lipocortins I and II belonging to the family of annexins. Antibodies raised against PP4, PAP III and p68 revealed to be highly specific, while those raised against PP4-X reacted with all investigated annexins, except PP4. Cross-reactivity was also observed between lipocortins I and II. All annexins inhibited in a concentration-dependent manner blood coagulation but with different potencies as was determined by means of a modified thromboplastin time test. The most potent inhibitors turned out to be PP4 and PAP III, followed by PP4-X, lipocortin I, p68 and lipocortin II.
Römisch
J
J
Forschungslaboratorien der Behringwerke AG, Marburg/Lahn.
Heimburger
N
N
D017304:Annexin A5; D017302:Annexins; D000906:Antibodies / Q000276:immunology; D000925:Anticoagulants / Q000302:isolation & purification; D002135:Calcium-Binding Proteins / Q000276:immunology / Q000302:isolation & purification*; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D007526:Isoelectric Point; D008970:Molecular Weight; D010920:Placenta / Q000032:analysis*; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000276:immunology / Q000302:isolation & purification*
D017304:Annexin A5; D017302:Annexins; D000906:Antibodies; D000925:Anticoagulants; D002135:Calcium-Binding Proteins; D011257:Pregnancy Proteins