Plasminogen, Glu, CHOII (Affinity Form II), Human

Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4mM (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=9x10e-6M) and four low affinity (Kd=5x10e-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of plasminogen with fibrin and a2-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. \n\nThe 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.\n\nAdditional Specifications:\nLocalization: Plasma \n\nPlasma Concentration: 2.4uM (4)\n\nMode of Action: Zymogen; precursor to the serine protease plasmin \n\nExtinction Coefficient: E1%1cm, 280nm=17.0 (5)\n\nIsoelectric Point: 6.2 (1)\n\nStructure: Single chain, 24 intra chain disulfide bridges, 5 kringle regions.\n \nPercent carbohydrate: ~2%

Prices direct from United States Biological

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

P4256-54

Size

1mg

Form

Supplied as a liquid in 50% glycerol/H2O.

Purity

(same/more than)95% by SDS-PAGE. 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). Determined by SDS-PAGE analysis.

References

1. Robbins, K.C., Methods in Enzymology, 45, 257 (1976).\n2. Collen, D. in Blood Coagulation, Zwaal, R.E.A. and Hemker, H.C., eds., pp. 243-258, New York, Elsevier (1986).\n3. Castellino, F.J., et al., Methods in Enzymology, 80, 365 (1981).\n4. Wohl, R.C., et al., Thromb. Res., 27 523 (1982).\n5. Barlow, G.H., et al., Biochemistry, 23, 2384 (1984).\n6. Sottrup-Jensen, L., et al., in Progress in Chemical Fibrinolysis and Thrombolysis, Vol. 3, ed. J.F. Davidson, R.M. Rowan, M.M. Samana, P.C. Desnoyers, pp. 197-228, New York: Raven Press (1975).