title: A rapid and simple method for the separation of four molecular forms of human plasminogen.
abstract: At least four molecular forms of plasminogen are known. Two of those forms have glutamic acid at their amino-terminal end, and are designated as glu-plasminogen. The other two have lysine, methionine and/or valine as amino-terminal amino acid and are collectively designated as lys-plasminogen. Two subforms (I and II) each of glu- and lys-plasminogen exist. The I-forms are glycosylated at asn-288 and thr-345, whereas the II-forms are only glycosylated at thr-345. In a previous publication (Thromb Haemostas 1984; 52: 347-349) we have described the separation of the I- and II-forms of plasminogen in lysine-Sepharose in phosphate buffers. Now we have combined those findings with the differential affinity of glu- and lys-plasminogen for aminohexyl-Sepharose through their aminohexyl-sites, recently described by Christensen (Biochem J 1984; 223: 431-421). Acid/urea electrophoresis, end-group determination and carbohydrate analysis show that the combination of affinity chromatography on lysine-Sepharose in phosphate buffers, and on aminohexyl-Sepharose provides an efficient procedure to separate the four molecular forms of plasminogen.
authors.affiliation: Gaubius Institute TNO, Leiden, The Netherlands.
authors.forename: W
authors.initials: W
authors.lastname: Nieuwenhuizen
authors.forename: D W
authors.initials: DW
authors.lastname: Traas
mesh_terms: D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D004586:Electrophoresis; D006801:Humans; D010446:Peptide Fragments / Q000302:isolation & purification*; D010958:Plasminogen / Q000302:isolation & purification*
chemical_list: D002241:Carbohydrates; D010446:Peptide Fragments; C018998:lysyl-plasminogen; D010958:Plasminogen