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A rapid and simple method for the separation of four molecular forms of human plasminogen

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Author: Nieuwenhuizen, W. · Traas, D.W.
Type:article
Date:1989
Institution: Gezondheidsorganisatie TNO Gaubius instituut TNO
Source:Thrombosis and haemostasis, 2, 61, 208-210
Identifier: 243701
Keywords: Affinity chromatography · Methodology · Carbohydrates · Chromatography, Affinity · Electrophoresis · Human · Peptide Fragments · 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. Chemicals/CAS: plasminogen, 9001-91-6; Carbohydrates; lysyl-plasminogen; Peptide Fragments; Plasminogen, 9001-91-6