https://journal.chestnet.org/article/S0012-3692(12)60129-9/pdf

Antithrombotic therapy for VTE disease: Antithrombotic Therapy and Prevention of Thrombosis, 9th ed: American College of Chest Physicians Evidence-Based Clinical Practice Guidelines.

Publisher Summary This chapter discusses the role of plasminogen activators in various biological processes. In specific, it describes two types of plasminogen activators—namely, the urokinase-type plasminogen activator (u-PA) and the tissue-type plasminogen activator (t-PA), which are essentially different gene products. The amino acid sequences of these activators and nucleotide sequences of the corresponding cDNAs have largely been determined, and the cDNAs have been cloned using recombinant techniques. A variety of enzymatic as well as immunological assay and detection methods have also been developed that allows a precise quantification of the activators, a distinction between u-PA and t-PA, determination of whether an activator is present in its active or zymogen form, analysis of the kinetics of different steps of the cascade reaction, and immunocytochemical identification of u-PA and t-PA in tissue sections. Much of the studies on plasminogen activators and cancer has been guided by the hypothesis that proteolysis of the components of extracellular matrix, initiated by the release of plasminogen activator from the cancer cells, plays a decisive role for the degradation of normal tissue, and thereby for invasive growth and metastases.

Plasminogen activators, tissue degradation, and cancer.

Plasminogen was prepared from human plasma by affinity chromatography on L-lysine-substituted Sepharose. Thirty milligrams of plasminogen, with a specific activity of 100 caseinolytic units (Committee on Thrombolytic Agents) per milligram of nitrogen, were obtained from 340 milliliters of plasma. This corresponds to over 200-fold purification from plasma. Disc-gel electrophoresis at pH 8.3 indicated seven distinct bands, all of which contained activity.

https://science.sciencemag.org/content/sci/170/3962/1095.full.pdf

Plasminogen: Purification from Human Plasma by Affinity Chromatography

Antithrombotic therapy for venous thromboembolic disease.

On the regulation and control of fibrinolysis. Edward Kowalski Memorial Lecture.

http://www.jbc.org/content/234/4/832.full.pdf

ε-Aminocaproic Acid: an Inhibitor of Plasminogen Activation

course of several years. The fact that the study is now in progress is in large part a result of extensive cooperation between the academic medical community, the pharmaceutical industryt and the National Heart Institute, the sponsoring agency. Following the first observation of the in vitro fibrinolytic activity of human urine by MacFarlane and Pilling' in 1947, this activity was identified as due to urokinase, a plasminogen (profibrinolysin) activator with

Sol Sherry

Papers

ε-Aminocaproic Acid: an Inhibitor of Plasminogen Activation

The urokinase-pulmonary embolism trial.

Serum transaminase activity; observations in a large group of patients.

The development of urokinase as a thrombolytic agent. maintenance of a sustained thrombolytic state in man by its intravenous infusion.

The activation of human plasminogen. I. Spontaneous activation in glycerol.