Antioxidant properties of high molecular weight dietary chitosan in vitro and in vivo

2011 ◽  
Vol 83 (2) ◽  
pp. 501-505 ◽  
Author(s):  
Makoto Anraku ◽  
Takeshi Fujii ◽  
Yuko Kondo ◽  
Eijiro Kojima ◽  
Toshiyuki Hata ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Antioxidant Properties

scholarly journals In Vitro Antioxidant Activity and FTIR Characterization of High-Molecular Weight Melanoidin Fractions from Different Types of Cocoa Beans

Antioxidants ◽  
2019 ◽  
Vol 8 (11) ◽  
pp. 560 ◽  
Author(s):  
Oracz ◽  
Zyzelewicz
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Antioxidant Properties ◽  
Model Systems ◽  
Total Phenolic ◽  
Cocoa Beans ◽  
Potential Health ◽  
Antioxidant Power ◽  
Different Types

Melanoidins from real foods and model systems have received considerable interest due to potential health benefits. However, due to the complexity of these compounds, to date, the exact structure of melanoidins and mechanism involved in their biological activity has not been fully elucidated. Thus, the aim of this study was to investigate the total phenolic content, antioxidant properties, and structural characteristics of high-molecular weight (HMW) melanoidin fractions isolated by dialysis (>12.4 kDa) from raw and roasted cocoa beans of Criollo, Forastero, and Trinitario beans cultivated in various area. In vitro antioxidant properties of all studied HMW cocoa fractions were evaluated by four different assays, namely free radical scavenging activity against DPPH● and ABTS●+ radicals, ferric reducing antioxidant power (FRAP), and metal-chelating ability. Additionally, the structure–activity relationship of isolated HMW melanoidin fractions were analyzed using attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). The results show that roasting at a temperature of 150 °C and a relative air humidity of 0.3% effectively enhances the total phenolics content and the antioxidant potential of almost all HMW cocoa melanoidin fractions. The ATR-FTIR analysis revealed that the various mechanisms of action of HMW melanoidins isolates of different types of cocoa beans related to their structural diversity. Consequently, the results clearly demonstrated that HMW cocoa fractions isolated from cocoa beans (especially those of Criollo variety) roasted at higher temperatures with the lower relative humidity of air possess high antioxidant properties in vitro.

In Vitro and in Vivo Antigen-Induced Release of High-Molecular Weight Neutrophil Chemotactic Activity from Human Nasal Tissue

1988 ◽  
Vol 2 (1) ◽  
pp. 7-11 ◽  
Author(s):  
T. Nagakura ◽  
T. Onda ◽  
Y. likura ◽  
T. Endo ◽  
H. Nagakura ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Nasal Polyps ◽  
Gel Filtration ◽  
Chemotactic Activity ◽  
Nasal Tissue ◽  
Nasal Secretions ◽  
Neutrophil Chemotactic Activity

High molecular weight neutrophil chemotactic activity has been identified in resected human nasal polyps, inferior turbinates, and nasal secretions following antigen challenge. The estimated molecular weight, by gel filtration chromatography, was approximately 600,000. However, a heterogeneity of molecular weight in some patients was recognized. Our results suggest a possible role for high molecular weight-neutrophil chemotactic activity in the pathogenesis of hypersensitivity in the human nasal cavity.

scholarly journals An Assessment of the Bioactivity of Coffee Silverskin Melanoidins

Foods ◽  
2019 ◽  
Vol 8 (2) ◽  
pp. 68 ◽  
Author(s):  
Silvia Tores de la Cruz ◽  
Amaia Iriondo-DeHond ◽  
Teresa Herrera ◽  
Yolanda Lopez-Tofiño ◽  
Carlos Galvez-Robleño ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Dietary Fiber ◽  
High Molecular Weight ◽  
Research Work ◽  
Weight Fraction ◽  
High Molecular Weight Fraction ◽  
Total Dietary Fiber ◽  
Coffee Silverskin

Melanoidins present in coffee silverskin, the only by-product of the roasting process, are formed via the Maillard reaction. The exact structure, biological properties, and mechanism of action of coffee silverskin melanoidins, remain unknown. This research work aimed to contribute to this novel knowledge. To achieve this goal, melanoidins were obtained from an aqueous extract of Arabica coffee silverskin (WO2013004873A1) and was isolated through ultrafiltration (>10 kDa). The isolation protocol was optimized and the chemical composition of the high molecular weight fraction (>10 kDa) was evaluated, by analyzing the content of protein, caffeine, chlorogenic acid, and the total dietary fiber. In addition, the structural analysis was performed by infrared spectroscopy. Antioxidant properties were studied in vitro and the fiber effect was studied in vivo, in healthy male Wistar rats. Melanoidins were administered to animals in the drinking water at a dose of 1 g/kg. At the fourth week of treatment, gastrointestinal motility was evaluated through non-invasive radiographic means. In conclusion, the isolation process was effective in obtaining a high molecular weight fraction, composed mainly of dietary fiber, including melanoidins, with in vitro antioxidant capacity and in vivo dietary fiber effects.

scholarly journals Arabidopsis Dynamin-Like 2 That Binds Specifically to Phosphatidylinositol 4-Phosphate Assembles into a High-Molecular Weight Complex in Vivo and in Vitro

2001 ◽  
Vol 127 (3) ◽  
pp. 1243-1255 ◽  
Author(s):  
Yong-Woo Kim ◽  
Dae-Sup Park ◽  
Seung-Cheol Park ◽  
Sung Hee Kim ◽  
Gang-Won Cheong ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
High Molecular Weight Complex ◽  
Phosphatidylinositol 4

scholarly journals MEKK1 activates both IκB kinase α and IκB kinase β

1998 ◽  
Vol 95 (16) ◽  
pp. 9319-9324 ◽  
Author(s):  
Frank S. Lee ◽  
Robert T. Peters ◽  
Luan C. Dang ◽  
Tom Maniatis
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Mitogen Activated Protein Kinase ◽  
Site Specific ◽  
Iκb Kinase ◽  
Mitogen Activated Protein ◽  
Bona Fide ◽  
Factor Α

A critical step in the signal-induced activation of the transcription factor NF-κB is the site-specific phosphorylation of its inhibitor, IκB, that targets the latter for degradation by the ubiquitin–proteasome pathway. We have previously shown that mitogen-activated protein kinase/ERK kinase kinase 1 (MEKK1) can induce both this site-specific phosphorylation of IκBα at Ser-32 and Ser-36 in vivo and the activity of a high molecular weight IκB kinase complex in vitro. Subsequently, others have identified two proteins, IκB kinase α (IKK-α) and IκB kinase β (IKK-β), that are present in a tumor necrosis factor α-inducible, high molecular weight IκB kinase complex. These kinases are believed to directly phosphorylate IκB based on the examination of the kinase activities of IKK immunoprecipitates, but more rigorous proof of this has yet to be demonstrated. We show herein that recombinant IKK-α and IKK-β can, in fact, directly phosphorylate IκBα at Ser-32 and Ser-36, as well as homologous residues in IκBβ in vitro, and thus are bona fide IκB kinases. We also show that MEKK1 can induce the activation of both IKK-α and IKK-β in vivo. Finally, we show that IKK-α is present in the MEKK1-inducible, high molecular weight IκB kinase complex and treatment of this complex with MEKK1 induces phosphorylation of IKK-α in vitro. We conclude that IKK-α and IKK-β can mediate the NF-κB-inducing activity of MEKK1.

FRACTIONATION OF LIVER SOMATOMEDIN ACTIVITY BY ULTRAFILTRATION

1974 ◽  
Vol 62 (2) ◽  
pp. 355-361 ◽  
Author(s):  
JENNIFER M. DEHNEL ◽  
P. D. McCONAGHEY ◽  
M. J. O. FRANCIS
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Weight Fraction ◽  
Low Molecular Weight ◽  
High Molecular Weight Fraction ◽  
Cartilage Growth ◽  
The Relationship ◽  
Somatomedin Inhibitors

SUMMARY Plasma somatomedin is the intermediary through which growth hormone (GH) exerts its effects on the growing skeleton. Somatomedin activity may be produced in vitro by perfusion of the liver and kidneys of rats with Waymouth's medium containing GH. The relationship between the activity of plasma somatomedin and somatomedin of hepatic and renal origin has yet to be clarified. Somatomedin from plasma can be separated into active fractions of both high and low molecular weight. Similarly, ultrafiltration of medium containing somatomedin of hepatic origin indicates the existence of two active fractions, one of high molecular weight (greater than 50000) and one of low molecular weight (less than 1000). The latter can be attributed to the release of amino acids, such as serine and glutamine, by the perfused tissue. The high molecular weight fraction is believed to represent GH-dependent somatomedin. Fractions that inhibit production of cartilage matrix are present in liver perfusates as well as in plasma. These results provide further evidence that the liver is a source of GH-dependent somatomedin in vivo. Furthermore, cartilage growth may be controlled not only by the GH-stimulated release of somatomedin by the liver, but also by its release of acid-labile somatomedin inhibitors.

The Fibrin Assay Comparison Trial (FACT)

2001 ◽  
Vol 85 (04) ◽  
pp. 671-678 ◽  
Author(s):  
Sybille Zips ◽  
Hanimsah Ergül ◽  
Dieter Heene ◽  
Carl-Erik Dempfle ◽  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Degradation Products ◽  
Plasma Samples ◽  
Fibrin Degradation Products ◽  
Comparison Trial ◽  
Clinical Conditions ◽  
D Dimer

SummaryAlthough D-dimer has gained widespread clinical use as a parameter for detection of in vivo fibrin formation, the issue of standardization of D-dimer assays remains to be resolved. The FACT study was performed to generate basic data for development of calibrators and standard preparations.A set of 86 samples, including plasma samples from patients with DIC, DVT, and other clinical conditions, serial dilutions of pooled plasma samples, and plasma samples containing fibrinogen- and fibrin derivatives, were distributed to 12 manufacturers of D-dimer assays.D-dimer assays differ concerning specificity for crosslinked fibrin, and preference for either high molecular weight fibrin complexes, or low molecular weight fibrin degradation products. Terminal plasmin digests of fibrin clots for calibration produce aberrant results in some assays, especially those with preference for high molecular weight crosslinked fibrin derivatives. The best conformity is achieved by the use of pooled plasma samples from patients with high levels of D-dimer antigen in plasma. In vitro preparations containing a comparable composition of fibrin derivatives to clinical plasma samples may also serve as reference material.

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