Interaction of streptokinase and plasminogen

Renzo, E.C. De; Barg, William F.; Boggiano, E.; Englert, Mary E.; Davies, M.C.

doi:10.1016/0006-291x(63)90243-2

Cited by 25 publications

(5 citation statements)

References 8 publications

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“…Our results also explain the literature discrepancy on the value of the sedimentation coefficient. The value of s = 10 S reported by Ling et al (1966) and Davies et al (1961) was on a Lys-plasmin-streptokinase complex with an available active site, while the s value near 5 S reported by De Renzo et al (1963) and Summaria et al (1970) was on the Lys-plasmin-streptokinase complex in which the active site was blocked.…”

Section: Discussionmentioning

confidence: 82%

Hydrodynamic studies on the streptokinase complexes of human plasminogen, Val442-plasminogen, plasmin, and the plasmin-derived light (B) chain

Barlow¹,

Summaria²,

Robbins³

1984

Biochemistry

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Sedimentation velocity and sedimentation equilibrium studies have been carried out on the Glu- and Lys-plasminogen-streptokinase complexes as well as on the complexes formed by Val442-plasmin and the light (B) chain of plasmin. Sedimentation equilibrium molecular weights are consistent with a 1 to 1 molar complex in all cases and give values consistent with the differences in size of the plasminogen moieties. Sedimentation velocity determinations in the presence of protease inhibitors give values consistent with the conformational differences already reported for the Glu- and Lys-plasminogen molecules. However, unlike Glu-plasminogen, the addition of epsilon-aminocaproic acid or lysine does not alter the conformation of the Glu-plasminogen complex. The values of the sedimentation coefficient and the molecular weight of the plasmin and the Val442-plasmin-streptokinase complexes increase to those of a dimer when determined in the absence of active-site inhibitors but return to monomer values when these inhibitors are added. Thus, dimer formation requires the presence of an available active site in at least one of the two molecules involved and is reversible.

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Section: Discussionmentioning

confidence: 82%

Hydrodynamic studies on the streptokinase complexes of human plasminogen, Val442-plasminogen, plasmin, and the plasmin-derived light (B) chain

Barlow¹,

Summaria²,

Robbins³

1984

Biochemistry

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“…Ratnoff (34) provided the first evidence that a stoichiometric reaction occurred between SK and a factor in human euglobulin which led to the activation of plasminogen. Later DeRenzo et al (11,12) demonstrated a SK-plasminogen complex by ultracentrifugation and starch gel electrophoresis . Eventually Ling, Summaria and Robbins (24) reported the isolation and characterization of such a complex from a mixture of SK and purified human p lasminogen.…”

Section: Discussionmentioning

confidence: 99%

Streptokinase and Urokinase Activation of Human, Chimpanzee and Baboon Plasminogen

McKee¹,

Lemmon²,

Hampton³

1971

Thromb Haemost

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SummaryHuman, chimpanzee and baboon plasminogens, in that order, were found to be decreasingly susceptible to streptokinase (SK) activation. The relative activation of the three primate plasminogens remained the same when species specific fibrin or casein was used as substrate and when the following conditions were varied: 1. SK concentration; 2. plasminogen concentration; and 3. length of incubation of the SK-plasminogen-substrate reaction mixture. Under the same conditions, the three primate plasminogens were readily activated by human urokinase (UK) and no consistent order of activation by UK was observed. Our findings suggest that the site on plasminogen which interacts with SK has undergone changes during evolution whereas the site at which UK activates each of the three plasminogens has changed little. It remains obscure whether the susceptibility of primate plasminogen to SK activation is a specifically selected genetic trait or is simply a laboratory indication of structural changes in the plasminogen molecule that have occurred for other reasons.

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“…De Renzo et al [2,6,7,8,10] have dedicated much of their work to the study of the plasminogen-streptokinase interaction. These authors used highly purified preparations and restricted their investigations to the human species; most of their studies were carried out in the presence of inhibitors of both plasminogen activator and plasmin.…”

Section: Discussionmentioning

confidence: 99%

“…The results of these experiments indicated that plasminogen and streptokinase are able to react stoichiometrically thereby forming complexes [2,6,7,8,10]. Most of these investigations were performed in presence of e-amino caproic acid, possibly in order to prevent an extensive breakdown of the components in volved in the reaction.…”

mentioning

confidence: 99%

Gel Filtration Studies of the Complex Forming Capacity of Streptokinase with Human and Heterologous Plasminogens

Doleschel¹,

Auerswald²,

Cranz³

et al. 1967

Pharmacology

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Interaction of streptokinase and plasminogen

Cited by 25 publications

References 8 publications

Hydrodynamic studies on the streptokinase complexes of human plasminogen, Val442-plasminogen, plasmin, and the plasmin-derived light (B) chain

Hydrodynamic studies on the streptokinase complexes of human plasminogen, Val442-plasminogen, plasmin, and the plasmin-derived light (B) chain

Streptokinase and Urokinase Activation of Human, Chimpanzee and Baboon Plasminogen

Gel Filtration Studies of the Complex Forming Capacity of Streptokinase with Human and Heterologous Plasminogens

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