Nattokinase Selected Abstracts:

Potent fibrinolytic enzyme from a mutant of Bacillus subtilis IMR-NK1.

Chang CT, Fan MH, Kuo FC, Sung HY. J Agric Food Chem 2000 Aug;48(8):3210-6 Department of Food and Nutrition, Providence University, Shalu, Taiwan, Republic of China.

A mutant of Bacillus subtilis IMR-NK1, which is used for the production of domestic "natto" in Taiwan, produced high fibrinolytic enzyme activity by solid-state fermentation using wheat bran as medium.

Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang.

Kim W, Choi K, Kim Y, Park H, Choi J, Lee Y, Oh H, Kwon I, Lee S. Appl Environ Microbiol 1996 Jul;62(7):2482-8 Department of Biotechnology, Institute of R & D, Yangpyung-Dong, Youngdeungpo-Gu, Seoul, (South) Korea. bio00@bora.dacom.co.kr

Bacillus sp. strain CK 11-4, which produces a strongly fibrinolytic enzyme, was screened from Chungkook-Jang, a traditional Korean fermented-soybean sauce. The fibrinolytic enzyme (CK) was purified from supernatant of Bacillus sp. strain CK 11-4 culture broth and showed thermophilic, hydrophilic, and strong fibrinolytic activity.

Thrombolytic effect of nattokinase on a chemically induced thrombosis model in rat.

Fujita M, Hong K, Ito Y, Fujii R, Kariya K, Nishimuro S. Biol Pharm Bull 1995 Oct;18(10):1387-91 Biotechnology Research Laboratories, JCR Pharmaceuticals Co., Ltd., Kobe, Japan.

Nattokinase is a new fibrinolytic enzyme which cleaves directly cross-linked fibrin in vitro. In this study, we investigated the thrombolytic effect of nattokinase on a thrombus in the common carotid artery of rat in which the endothelial cells of the vessel wall were injured by acetic acid. When a section of occluded vessel was stained for CD61 antigen by immunofluorescence utilizing a monoclonal antibody, the antigen was localized around the surface of the occluded blood vessels. This result suggests that the occlusive thrombosis was caused by platelet aggregation. In addition, thrombolysis with urokinase (UK; 50000 IU/kg, i.v.) or tissue plasminogen activator (tPA; 13300 IU/kg, i.v.) in our model was observed to restore the blood flow over a 60 min monitoring period. The results indicate that our chemically induced model is useful for screening and evaluating a thrombolytic agent. We evaluated the thrombolytic activity of nattokinase using this model and compared it with fibrino(geno)lytic enzyme, plasmin or elastase. On a molar basis, the recovery of the arterial blood flow with nattokinase, plasmin and elastase were 62.0 +/- 5.3%, 15.8 +/- 0.7% and 0%, respectively. The results indicate that the thrombolytic activity of nattokinase is stronger than that of plasmin or elastase in vivo.

Transport of nattokinase across the rat intestinal tract.

Fujita M, Hong K, Ito Y, Misawa S, Takeuchi N, Kariya K, Nishimuro S. Biol Pharm Bull 1995 Sep;18(9):1194-6 Biotechnology Research Laboratories, JCR Pharmaceuticals Co., Ltd., Kobe, Japan.

Intraduodenal administration of nattokinase (NK) at a dose of 80 mg/kg, resulted in the degradation of fibrinogen in plasma suggesting transport of NK across the intestinal tract in normal rats. The action of NK on the cleavage of fibrinogen in the plasma from blood samples drawn at intervals after intraduodenal administration of the enzyme was investigated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting analysis with an anti-fibrinogen gamma chain antibody. In parallel with the degradation process, plasma recalcification times were remarkably prolonged NK was also detected in the plasma from blood samples drawn 3 and 5 h after administration of the enzyme by SDS-PAGE and Western blotting analysis with an anti-NK antibody. The results indicate that NK is absorbed from the rat intestinal tract and that NK cleaves fibrinogen in plasma after intraduodenal administration of the enzyme.

Purification and characterization of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese natto, a popular soybean fermented food in Japan.

Fujita M, Nomura K, Hong K, Ito Y, Asada A, Nishimuro S. Biochem Biophys Res Commun 1993 Dec 30;197(3):1340-7 Biotechnology Research Laboratories, JCR Pharmaceuticals Co., Ltd., Kobe, Japan.

A strong fibrinolytic enzyme (nattokinase) was purified from the vegetable cheese natto. Nattokinase was extracted from natto with saline and isolated by sequential use of hydrophobic chromatography. The isolated protein gave a single sharp band on SDS-PAGE either before or after reduction. The sequence, as determined by automated Edman degradation of the uncleaved molecule and its enzymatically derived peptide, consisted of a total 275 amino acid residues (M.W = 27,728) and exhibited a high homology with the subtilisins.

Enhancement of the fibrinolytic activity in plasma by oral administration of nattokinase.

Sumi H, Hamada H, Nakanishi K, Hiratani H. Acta Haematol 1990;84(3):139-43 Department of Physiology, Miyazaki Medical College, Japan.

The existence of a potent fibrinolytic enzyme (nattokinase, NK) in the traditional fermented food called 'natto', was reported by us previously. It was confirmed that oral administration of NK (or natto) produced a mild and frequent enhancement of the fibrinolytic activity in the plasma, as indicated by the fibrinolytic parameters, and the production of tissue plasminogen activator. NK capsules were also administered orally to dogs with experimentally induced thrombosis, and lysis of the thrombi was observed by angiography. The results obtained suggest that NK represents a possible compound for use not only in the treatment of embolism but also in the prevention of the disease, since NK has a proven safety and can be massproduced.

A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet.

Sumi H, Hamada H, Tsushima H, Mihara H, Muraki H. Experientia 1987 Oct 15;43(10):1110-1 Department of Physiology, Miyazaki Medical College, Japan.

A strong fibrinolytic activity was demonstrated in the vegetable cheese Natto, which is a typical soybean food eaten in Japan. The average activity was calculated at about 40 CU (plasmin units)/g wet weight. This novel fibrinolytic enzyme, named nattokinase, was easily extracted with saline. Nattokinase not only digested fibrin, but also the plasmin substrate H-D-Val-Leu-Lys-pNA (S-2251).

 

 

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