glu-Plasminogen, lys-Plasminogen and carbohydrate variants

Human Plasminogen
The domain structure of human plasminogen is represented where: K1-K5 = the 5 kringle domains, B-CHAIN = catalytic domain of plasmin , and the arrows indicate the sites of proteolytic cleavage by plasmin, elastase, and plasminogen activators (PA’S).

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Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 µM (1,2). The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9×10-6M) and four low affinity (Kd=5×10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of plasminogen with fibrin and α2-antiplasmin is mediated by these lysine binding sites. Native glu-plasminogen (Mr=88,000) is readily converted to Lys-77-plasminogen (Mr=83,000) by plasmin hydrolysis of the Lys76-Lys77 peptide bond. Elastase catalyzed cleavage of the Val441-Val442 peptide bond of glu-plasminogen yields a functionally active zymogen termed Val-442 plasminogen or mini-plasminogen.

The conversion of plasminogen to plasmin occurs by a variety of mechanisms, but all result in hydrolysis of the Arg560-Val561 peptide bond of plasminogen, yielding two chains which remain covalently associated by a disulfide bond.

Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino (3), utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid (3). The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20oC. Purity is determined by SDS-PAGE analysis.

Sample gel image
Lane 1Human Glu-Plasminogen (HCPG-0130) Reduced
Lane 2Human Glu-Plasminogen CHOI (HCPG-0131) Reduced
Lane 3Human Glu-Plasminogen CHOII (HCPG-0132) Reduced
Lane 4Human Lys-Plasminogen (HCPG-0133) Reduced
Marker: See Blue +2_MOPS
Lane 5Human Glu-Plasminogen (HCPG-0130) Non-Reduced
Lane 6HumanGlu-Plasminogen CHOI (HCPG-0131) Non-Red
Lane 7Human Glu-Plasminogen CHOII (HCPG-0132) Non-Red
Lane 8Human Lys-Plasminogen (HCPG-0133) Non-Reduced
GelNovex 4-12% Bis-Tris
Load1 µg per lane
StandardSeeBluePlus 2; Myosin (191 kDa), Phosphorylase B (97 kDa), BSA (64 kDa), Glutamic Dehydrogenase (51 kDa), Alcohol Dehydrogenase (39 kDa), Carbonic Anhydrase (28 kDa), Myoglobin Red (19 kDa), Lysozyme (14 kDa)
Plasma concentration2.4 µM (human) (4)
Mode of actionZymogen; precursor to the serine protease plasmin
Molecular weight88,000 (glu plasminogen) (5)
83,000 (lys-plasminogen) (5)
38,000 (val-plasminogen) (6)
Extinction coefficient
1 %
1 c m, 280 nm
= 17.0 (5)
Isoelectric point6.2 (glu-plasminogen) (1)
6.7-8.3 (lys-plasminogen) (1)
Structuresingle chain, 24 intra chain disulfide bridges, 5 kringle regions.
Percent carbohydrateApproximately 2%
  1. Robbins, K.C., Methods in Enzymology, 45, 257 (1976).
  2. Collen, D. in Blood Coagulation, Zwaal, R.E.A. and Hemker, H.C., eds., pp. 243-258, New York, Elsevier (1986).
  3. Castellino, F.J., et al., Methods in Enzymology, 80, 365 (1981).
  4. Wohl, R.C., et al., Thromb. Res., 27 523 (1982).
  5. Barlow, G.H., et al., Biochemistry, 23, 2384 (1984).
  6. Sottrup-Jensen, L., et al., in Progress in Chemical Fibrinolysis and Thrombolysis, Vol. 3, ed. J.F. Davidson, 7. R.M. Rowan, M.M. Samana, P.C. Desnoyers, pp. 197-228, New York: Raven Press (1975).
  1. Zaas AK, Liao G, Chien JW, Weinberg C, Shore D, et al. (2008) Plasminogen Alleles Influence Susceptibility to Invasive Aspergillosis. PLoS Genet 4(6): e1000101.doi:10.1371/journal.pgen.1000101 (mouse plasminogen)

This publication list is not all encompassing, and is only meant to provide limited examples of how Prolytix products are used. We encourage you to search the literature for other examples pertinent to your experimentation, and to contact us with any technical questions.

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