Page last updated: 2024-08-26

fibrinogen and nattokinase

fibrinogen has been researched along with nattokinase in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (14.29)18.2507
2000's3 (42.86)29.6817
2010's2 (28.57)24.3611
2020's1 (14.29)2.80

Authors

AuthorsStudies
Fujita, M; Hong, K; Ito, Y; Kariya, K; Misawa, S; Nishimuro, S; Takeuchi, N1
Akita, S; Ihara, H; Oike, M; Suzuki, I; Suzuki, Y; Takada, A; Tsukamoto, Y; Umemura, K; Urano, T1
Huang, Q; Peng, Y; Zhang, RH; Zhang, YZ1
Cham, TM; Hsia, CH; Hwang, KL; Lin, JS; Shen, MC; Wen, YK; Yang, NC1
Fujita, M; Fukuyama, R; Nakamuta, H; Ogasawara, K; Ohnishi, K; Takaoka, S1
Clark, JF; Esaki, K; Hamaoka, T; Homma, T; Kurosawa, Y; Nirengi, S; Ohta, M1
Purwaeni, E; Retnoningrum, DS; Riani, C1

Trials

2 trial(s) available for fibrinogen and nattokinase

ArticleYear
Nattokinase decreases plasma levels of fibrinogen, factor VII, and factor VIII in human subjects.
    Nutrition research (New York, N.Y.), 2009, Volume: 29, Issue:3

    Topics: Adult; Aged; Cholesterol; Factor VII; Factor VIII; Female; Fibrinogen; Humans; Male; Middle Aged; Subtilisins; Young Adult

2009
A single-dose of oral nattokinase potentiates thrombolysis and anti-coagulation profiles.
    Scientific reports, 2015, Jun-25, Volume: 5

    Topics: Antithrombins; Blood Coagulation; Blood Coagulation Tests; Cross-Over Studies; Double-Blind Method; Factor VIII; Fibrin; Fibrin Fibrinogen Degradation Products; Fibrinogen; Fibrinolysis; Fibrinolytic Agents; Humans; Male; Partial Thromboplastin Time; Subtilisins; Time Factors

2015

Other Studies

5 other study(ies) available for fibrinogen and nattokinase

ArticleYear
Transport of nattokinase across the rat intestinal tract.
    Biological & pharmaceutical bulletin, 1995, Volume: 18, Issue:9

    Topics: Animals; Biological Transport; Fibrinogen; Fibrinolytic Agents; Intestinal Mucosa; Male; Molecular Weight; Rabbits; Rats; Rats, Wistar; Serine Endopeptidases; Subtilisins

1995
The profibrinolytic enzyme subtilisin NAT purified from Bacillus subtilis Cleaves and inactivates plasminogen activator inhibitor type 1.
    The Journal of biological chemistry, 2001, Jul-06, Volume: 276, Issue:27

    Topics: Bacillus subtilis; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fibrin; Fibrinogen; Fibrinolysis; Humans; Molecular Weight; Peptide Mapping; Plasminogen Activator Inhibitor 1; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Subtilisins

2001
Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food.
    Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 2003, Volume: 134, Issue:1

    Topics: Amino Acid Sequence; Bacillus; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Fibrinogen; Fibrinolytic Agents; Glycine max; Humans; Hydrogen-Ion Concentration; Isoelectric Focusing; Molecular Sequence Data; Protein Structure, Tertiary; Serine Endopeptidases; Subtilisin; Subtilisins; Temperature; Thrombin; Urokinase-Type Plasminogen Activator

2003
Antihypertensive effects of continuous oral administration of nattokinase and its fragments in spontaneously hypertensive rats.
    Biological & pharmaceutical bulletin, 2011, Volume: 34, Issue:11

    Topics: Administration, Oral; Angiotensin II; Animals; Antihypertensive Agents; Blood Pressure; Fibrinogen; Glycine max; Hypertension; Intestinal Absorption; Male; Peptide Hydrolases; Phytotherapy; Plant Extracts; Rats; Rats, Inbred SHR; Soy Foods; Subtilisins

2011
Molecular Characterization of Bacterial Fibrinolytic Proteins from Indonesian Traditional Fermented Foods.
    The protein journal, 2020, Volume: 39, Issue:3

    Topics: Amino Acid Substitution; Bacterial Proteins; Calcium; Cations, Divalent; Cations, Monovalent; Cloning, Molecular; Coenzymes; Escherichia coli; Fermented Foods; Fibrinogen; Fibrinolysis; Gene Expression; Genetic Vectors; Humans; Hydrogen-Ion Concentration; Potassium; Recombinant Proteins; Sodium; Subtilisins; Temperature

2020