Anticoagulant from Taraxacum platycarpum

• Published in: Bioscience, biotechnology, and biochemistry Vol. 66; no. 9; pp. 1859 - 1864
• Main Authors: "Yun, S.I. (University of Ulsan (Korea R.)), Cho, H.R, Choi, H.S.
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.09.2002; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Animals; ANTICOAGULANTS; Anticoagulants - chemistry; Anticoagulants - isolation & purification; Anticoagulants - pharmacology; anticoagulatory; antithrombotic; Biological and medical sciences; Blood Coagulation - drug effects; Cell Line; Cyclooxygenase 2; Drug Stability; Drugs, Chinese Herbal; FIBRINOGEN; General pharmacology; Hot Temperature; Isoenzymes - metabolism; Kallikreins - antagonists & inhibitors; Kallikreins - metabolism; LIGASES; LYASES; Macrophage Activation - drug effects; Macrophages - drug effects; Macrophages - enzymology; Macrophages - metabolism; Medical sciences; Mice; Molecular Weight; NITRIC OXIDE; nitric oxide synthase; Nitric Oxide Synthase - metabolism; Partial Thromboplastin Time; Pharmacognosy. Homeopathy. Health food; PHARMACOLOGY; Pharmacology. Drug treatments; Prostaglandin-Endoperoxide Synthases - metabolism; PROTEINS; Prothrombin Time; TARAXACUM; Taraxacum - chemistry; Taraxacum platycarpum; Thrombin - antagonists & inhibitors; Thrombin - metabolism; Thrombin Time; THROMBOSIS; Tumor Necrosis Factor-alpha - metabolism; Purification; Pharmacognosy; Anticoagulant; Compositae; In vitro; Taraxacum; Biological activity; Medicinal plant; Chinese medicine; Folk medicine; Dicotyledones; Angiospermae; Plant origin; Antithrombotic agent; Spermatophyta; Fibrinolytic
• DOI: 10.1271/bbb.66.1859
• ISSN: 0916-8451

"An anticoagulant was purified from a Chinese herb, Taraxacum platycarpum. Its activity was heat-Iabile, and was decreased by incubation with subtilisin Carlburg or proteinase K, indicating that the active component was a protein. The protein had a molecular mass of 31 kDa by gel filtration and 33 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis, so it probably was a monomer. When present at the concentration of 70, 255, and 873 nM, respectively, the protein doubled the thrombin time, prothrombin time, and activated partial thromboplastin time. It inhibited thrombin and kallikrein, but did not hydrolyze fibrinogen. The protein bound the anion-binding exosite of thrombin, competing with the fibrinogen binding site. In addition, the protein caused the murine macrophage cell line Raw 264.7 to produce cyclooxygenase-2, nitric oxide synthase, nitric oxide, and tumor necrosis factor-alpha. "