scholarly journals The Effects of Sorbus aucuparia L. Fruit Extracts on Oxidative/Nitrative Modifications of Human Fibrinogen, Impact on Enzymatic Properties of Thrombin, and Hyaluronidase Activity In Vitro

Antioxidants ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 2009
Author(s):  
Magdalena Rutkowska ◽  
Joanna Kolodziejczyk-Czepas ◽  
Monika Anna Olszewska
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cardiovascular Complications ◽  
Synergistic Activity ◽  
Sorbus Aucuparia ◽  
Human Fibrinogen ◽  
Structural Modifications ◽  
Hydroxycinnamic Acid Derivatives ◽  
Health Promoting

Sorbus aucuparia L. fruits (rowanberries) are food products with acknowledged nutritional value, high phenolic content, and traditional application in diabetes. In this study, the effects of rowanberry extracts (phytochemically standardised, i.a., by LC-MS/MS) on some aspects of plasma haemostasis and vascular conditions were evaluated in vitro as possible mechanisms connected with cardiovascular complications of diabetes. The analyses of structural modifications of human fibrinogen under oxidative stress conditions (C-ELISA, SDS-PAGE and Western blot) revealed that the extracts (at a concentration of 1–5 µg/mL) considerably reduced the nitration of tyrosine residues and formation of high-molecular-weight aggregates. Moreover, they inhibited the enzymatic activity of thrombin (both amidolytic and proteolytic). Additionally, some promising outcomes might be expected regarding endothelial functions from the extracts ability to inhibit hyaluronidase. Parallel experiments on model polyphenols and correlation studies formed the basis for determining the contribution of different compounds, including hydroxycinnamic acid derivatives, flavonols, and low- or high-molecular-weight flavan-3-ols derivatives (proanthocyanidins), to the observed effects. The possible synergistic activity of individual constituents was also noticed. These results broaden the knowledge on the biological activity of rowanberries, partly confirming their health-promoting properties, and indicating that their functional applications might be promising.

The Action of Brinase in Vitro and in Vivo

1975 ◽  
Author(s):  
P. J. Gaffney ◽  
K. Lord ◽  
R. D. Thornes
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Size Range ◽  
Degradation Products ◽  
Molecular Size ◽  
Human Fibrinogen ◽  
Rate Limiting Step ◽  
Rate Limiting

Brinase (an extract of Aspergillus Oryzae) was shown to rapidly digest human fibrinogen in vitro to aggregable degradation products with a molecular size range of 310,000 to 230,000 the latter fragments being more slowly digested to core fragments, Dbr and Ebr. The fibrinogen polypeptide chain susceptibility to Brinase attack was in the order Aα, γ, Bβ, Lysis of the Bβ chain seems to be the rate limiting step in the conversion of the high molecular weight fragments (MW 310,000–230,000) to the core fragments Dbr and Ebr. The conservation of NH2 terminal Tyrosine during fibrinogen digestion and the very transient existence of D dimer fragments during totally crosslinked fibrin lysis suggest that the carboxy end of the γ chain is prone to Brinase attack. The crosslinked α chains of fibrin, while resistant to plasmin, are vigorously digested by Brinase. The plasma of cancer patients being treated with Brinase contained degraded fibrinogen (lacking intact Aα chains) and their aggregates. These aggregates contained some crosslinked γ chains (γ-γ dimers) suggesting that Brinase in vivo exorcises both a lytic and coagulant effect. Thrombin mediated clots in all the plasmas examined contained no crosslinked α chains. Positive plasma ethanol gelation tests can be explained by the presence of the aggregable high molecular weight fragments observed during the in vitro lysis of fibrinogen by Brinase.

The Effect of Dextran of Various Molecular Weight on the Coagulation in Dogs

1961 ◽  
Vol 06 (01) ◽  
pp. 015-024 ◽  
Author(s):  
Sven Erik Bergentz ◽  
Oddvar Eiken ◽  
Inga Marie Nilsson
Keyword(s):  
Molecular Weight ◽  
Body Weight ◽  
High Molecular Weight ◽  
Bleeding Time ◽  
Factor Vii ◽  
Low Molecular Weight ◽  
Factor V ◽  
Coagulation Mechanism ◽  
Coagulation Defects

Summary1. Infusions of low molecular weight dextran (Mw = 42 000) to dogs in doses of 1—1.5 g per kg body weight did not produce any significant changes in the coagulation mechanism.2. Infusions of high molecular weight dextran (Mw = 1 000 000) to dogs in doses of 1—1.5 g per kg body weight produced severe defects in the coagulation mechanism, namely prolongation of bleeding time and coagulation time, thrombocytopenia, pathological prothrombin consumption, decrease of fibrinogen, prothrombin and factor VII, factor V and AHG.3. Heparin treatment of the dogs was found to prevent the decrease of fibrinogen, prothrombin and factor VII, and factor V otherwise occurring after injection of high molecular weight dextran. Thrombocytopenia was not prevented.4. In in vitro experiments an interaction between fibrinogen and dextran of high and low molecular weight was found to take place in systems comprising pure fibrinogen. No such interaction occurred in the presence of plasma.5. It is concluded that the coagulation defects induced by infusions of high molecular weight dextran are due to intravascular coagulation.

scholarly journals Physicochemical and Antifungal Properties of Clotrimazole in Combination with High-Molecular Weight Chitosan as a Multifunctional Excipient

Marine Drugs ◽  
2020 ◽  
Vol 18 (12) ◽  
pp. 591
Author(s):  
Bożena Grimling ◽  
Bożena Karolewicz ◽  
Urszula Nawrot ◽  
Katarzyna Włodarczyk ◽  
Agata Górniak
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Weight Ratio ◽  
Scanning Calorimetry ◽  
Minimal Inhibitory Concentrations ◽  
Dissolution Tests ◽  
Effective Combination ◽  
The Impact ◽  
High Molecular Weight Chitosan

Chitosans represent a group of multifunctional drug excipients. Here, we aimed to estimate the impact of high-molecular weight chitosan on the physicochemical properties of clotrimazole–chitosan solid mixtures (CL–CH), prepared by grinding and kneading methods. We characterised these formulas by infrared spectroscopy, differential scanning calorimetry, and powder X-ray diffractometry, and performed in vitro clotrimazole dissolution tests. Additionally, we examined the antifungal activity of clotrimazole–chitosan mixtures against clinical Candida isolates under neutral and acid conditions. The synergistic effect of clotrimazole and chitosan S combinations was observed in tests carried out at pH 4 on Candida glabrata strains. The inhibition of C. glabrata growth reached at least 90%, regardless of the drug/excipient weight ratio, and even at half of the minimal inhibitory concentrations of clotrimazole. Our results demonstrate that clotrimazole and high-molecular weight chitosan could be an effective combination in a topical antifungal formulation, as chitosan acts synergistically with clotrimazole against non-albicans candida strains.

scholarly journals Identity and Origin of the ATPase activity associated with neuronal microtubules. I. The ATPase activity is associated with membrane vesicles.

1983 ◽  
Vol 96 (5) ◽  
pp. 1298-1305 ◽  
Author(s):  
D B Murphy ◽  
R R Hiebsch ◽  
K T Wallis
Keyword(s):  
Molecular Weight ◽  
Atpase Activity ◽  
High Molecular Weight ◽  
Brain Tissue ◽  
Membrane Vesicles ◽  
Microtubule Associated Proteins ◽  
In Vitro Assembly ◽  
Microtubule Protein ◽  
Associated Proteins

Microtubule protein purified from brain tissue by cycles of in vitro assembly-disassembly contains ATPase activity that has been postulated to be associated with microtubule-associated proteins (MAPs) and therefore significant for studies of microtubule-dependent motility. In this paper we demonstrate that greater than 90% of the ATPase activity is particulate in nature and may be derived from contaminating membrane vesicles. We also show that the MAPs (MAP-1, MAP-2, and tau factors) and other high molecular weight polypeptides do not contain significant amounts of ATPase activity. These findings do not support the concept of "brain dynein" or of MAPs with ATPase activity.

Interaction of Streptococcus mutans Glucosyltransferases with Teichoic Acids

1980 ◽  
Vol 29 (2) ◽  
pp. 376-382
Author(s):  
H. K. Kuramitsu ◽  
L. Wondrack ◽  
M. McGuinness
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Streptococcus Mutans ◽  
Teichoic Acid ◽  
Lipoteichoic Acid ◽  
Water Soluble ◽  
Heat Inactivation ◽  
Teichoic Acids ◽  
Insoluble Glucan

The Streptococcus mutans GS5 glucosyltransferase activities (both water-soluble and -insoluble glucan-synthesizing fractions) were inhibited by purified lipoteichoic acid. In vitro sucrose-dependent colonization of smooth surfaces by strain GS5 was also markedly reduced in the presence of the amphipathic molecules. The inhibition of soluble glucan synthesis by lipoteichoic acid appeared to be competitive with respect to both sucrose and primer dextran T10. These inhibitory effects were dependent on the presence of the fatty acid components of lipoteichoic acid since deacylated lipoteichoic acids did not inhibit glucosyltransferase activity. However, the deacylated molecules did interact with the enzymes since deacylated lipoteichoic acid partially protected the enzyme activity against heat inactivation and also induced the formation of high-molecular-weight enzyme complexes from the soluble glucan-synthesizing fraction. The presence of teichoic acid in high-molecular-weight aggregates of glucosyltransferase isolated from the culture fluids of strain GS5 was suggested by the detection of polyglycerophosphate in these fractions. In addition to strain GS5, two other organisms containing polyglycerophosphate teichoic acids, Lactobacillus casei and Lactobacillus fermentum , were demonstrated to bind glucosyltransferase activity. These results are discussed relative to the potential role of teichoic acid-glucosyltransferase interactions in enzyme binding to the cell surface of S. mutans and the formation of high-molecular-weight enzyme aggregates in the culture fluids of the organism.

Preparation of high-molecular weight and high-sulfate content chitosans and their potential antioxidant activity in vitro

2005 ◽  
Vol 61 (2) ◽  
pp. 148-154 ◽  
Author(s):  
Ronge Xing ◽  
Song Liu ◽  
Huahua Yu ◽  
Zhanyong Guo ◽  
Zhien Li ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Antioxidant Activity ◽  
High Molecular Weight ◽  
Sulfate Content ◽  
High Sulfate

Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor

2013 ◽  
Vol 394 (3) ◽  
pp. 385-391 ◽  
Author(s):  
Thomas Kryza ◽  
Gilles Lalmanach ◽  
Marion Lavergne ◽  
Fabien Lecaille ◽  
Pascale Reverdiau ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Endothelial Cells ◽  
High Molecular Weight ◽  
High Molecular Weight Kininogen ◽  
Kinin Receptor ◽  
Angiogenic Effect ◽  
Lung Endothelial Cells ◽  
Carboxy Terminal

Abstract Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release.

scholarly journals Rat platelets activate high molecular weight atrial natriuretic peptides in vitro.

Hypertension ◽  
1985 ◽  
Vol 7 (6_pt_1) ◽  
pp. 905-912 ◽  
Author(s):  
N C Trippodo ◽  
A Januszewicz ◽  
B L Pegram ◽  
F E Cole ◽  
N Kohashi ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Natriuretic Peptides ◽  
Atrial Natriuretic Peptides ◽  
Rat Platelets ◽  
Atrial Natriuretic
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