The streptokinase-human plasminogen activator complex. Composition and identity of a subcomponent with activator activity.

نویسندگان

  • R H Tomar
  • F B Taylor
چکیده

Reactions between purified plasminogen and streptokinase, labelled with (131)I and (125)I respectively, were investigated by polyacrylamide-gel discontinuous electrophoresis. A molecular complex consisting of both (131)I-labelled plasminogen and (125)I-labelled streptokinase migrated between plasminogen and streptokinase. This complex contained bovine plasminogen activator activity. The relative quantities of (131)I-labelled plasminogen and (125)I-labelled streptokinase in this complex were markedly affected by reaction conditions. A fragment that retained 50% or more of the parent activator activity was released from the complex after exposure to mercaptoethanol. This subcomponent had an estimated molecular weight of 70000, and contained both (131)I-labelled plasminogen and (125)I-labelled streptokinase.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Interaction of Streptokinase and Human Plasminogen. I. Combining of Streptokinase and Plasminogen Observed in the Ultracentrifuge under a Variety of Experimental Conditions.

The activation of human plasminogen by streptokinase has been the subject of extensive investigation (4-8). There appears to be general agreement that at least two enzymatic activities are demonstrable in streptokinase-plasminogen reaction mixtures. One is the proteolytic enzyme human plasmin, characterized in part by its ability to hydrolyze lysine and arginine esters and protein substrates su...

متن کامل

Isolation of a human plasmin-derived, functionally active, light (B) chain capable of forming with streptokinase an equimolar light (B) chain-streptokinase complex with plasminogen activator activity.

A functionally active human plasmin light (B) chain derivative, stabilized by the streptomyces plasmin inhibitor leupeptin, was isolated from a partially reduced and alkylated enzyme preparation by an affinity chromatography method with a L-lysine-substituted Sepharose column. This light (B) chain derivative was found to be relatively homogeneous by electrophoretic analysis in both an acrylamid...

متن کامل

Optimizing refolding condition for recombinant tissue plasminogen activator

Low molecular size additives such as L-arginine and the redox compounds have been used both in the culturemedium and in vitro refolding to increase recombinant proteins production. Additives increase proteinrefolding and yield of active proteins by suppressing aggregate formation or enhancing refolding process.In this work, a comparative study was performed on refolding of rec...

متن کامل

ATP-regulated activity of the plasmin-streptokinase complex: a novel mechanism involving phosphorylation of streptokinase.

Streptokinase, an extracellular protein produced by Streptococci, is capable of activating the human fibrinolytic zymogen plasminogen. The rate of amidolytic activity of the plasminogen-streptokinase complex is greatly diminished by micromolar concentrations of ATP and heparin oligosaccharides. In addition, the plasminogen activator activity of the plasminogen-streptokinase complex is also inhi...

متن کامل

Comparison of the esterase and human plasminogen activator activities of various activated forms of human plasminogen and their equimolar streptokinase complexes.

A comparison was made of the esterase and activator activities of the various activated forms of human plasminogen and their streptokinase complexes with Nalpha-Cbz-L-lysine-p-nitrophenyl ester as the substrate. The steady state kinetic properties of Glu- and Lys-plasmins, and Glu- and Lys-plasminogen-streptokinase complexes were identical, while the Lys-plasmin-streptokinase complex showed a 2...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Biochemical journal

دوره 125 3  شماره 

صفحات  -

تاریخ انتشار 1971