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Thromb Haemost 1989; 61(02): 208-210
DOI: 10.1055/s-0038-1646560
Original Article
Schattauer GmbH Stuttgart

A Rapid and Simple Method for the Separation of Four Molecular Forms of Human Plasminogen

W Nieuwenhuizen
The Gaubius Institute TNO, Leiden, The Netherlands
,
D W Traas
The Gaubius Institute TNO, Leiden, The Netherlands
› Author Affiliations
Further Information

Publication History

Received 21 September 1988

Accepted after revision 01 December 1988

Publication Date:
30 June 2018 (online)

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Summary

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.

Keywords

Plasminogen - Affinity chromatography - Lysine-Sepharose - Aminohexyl-Sepharose
 

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