scholarly journals Allocolchicinoids bearing a Michael acceptor fragment for possible irreversible binding of tubulin

2020 ◽  
Vol 11 (6) ◽  
pp. 696-706
Author(s):  
Ekaterina S. Sazanova ◽  
Iuliia A. Gracheva ◽  
Diane Allegro ◽  
Pascale Barbier ◽  
Sébastien Combes ◽  
...  
Keyword(s):  
Covalent Binding ◽  
Irreversible Binding ◽  
Highly Active ◽  
Michael Acceptor ◽  
Sar Analysis

We describe an attempt to apply the concept of covalent binding towards the highly active allocolchicinoids selected on the basis of SAR analysis of previously synthesized molecules.

scholarly journals Fluorescent Whitening Agents. II. Covalent Binding to Proteins during Irradiation by Sunlight

1974 ◽  
Vol 27 (1) ◽  
pp. 23 ◽  
Author(s):  
LA Holt ◽  
B Milligan
Keyword(s):  
Aqueous Solution ◽  
Solid State ◽  
Bovine Serum Albumin ◽  
Photochemical Reaction ◽  
Covalent Binding ◽  
Covalent Bond ◽  
Solar Irradiation ◽  
Irreversible Binding ◽  
Fluorescent Whitening Agents ◽  
Simulated Solar Irradiation

Simulated solar irradiation of wool, silk, bovine serum albumin and apomyoglobin in the presence of radioactively labelled fluorescent whitening agents of the bistriazinylaminostilbene and pyrazoline types results in the irreversible binding of radioactivity to the protein. This photochemical reaction occurs both in the solid state and in aqueous solution, and is believed to result in the formation of a covalent bond between the whitener (or a photodecomposition product) and the protein.

scholarly journals Building Functional Surfaces for Biosensors Development

2013 ◽  
Vol 543 ◽  
pp. 204-207
Author(s):  
Carlos Morón ◽  
Alfonso Garcia ◽  
Enrique Tremps ◽  
Jose Andrés Somolinos
Keyword(s):  
Textile Industry ◽  
Physical Adsorption ◽  
Covalent Binding ◽  
Covalent Attachment ◽  
Layer By Layer ◽  
Protein Patterns ◽  
Highly Active ◽  
Pulp Paper ◽  
Potential Applications ◽  
Protein Resistant

Polyelectrolyte multilayers (PEM) built by layer-by-layer technique have been extensively studied over the last years, resulting in a wide variety of current and potential applications. This technique can be used to construct thin films with different functionalities, or to functionalize surfaces with substantial different properties of those of the underlying substrates. The multilayering process is achieved by the alternate adsorption of oppositely charged polyelectrolytes. In this work we get advantage of the protein resistant property of the Poly (l-lysine)-graft-(polyethyleneglycol) to create protein patterns. Proteins can be immobilized on a surface by unspecific physical adsorption, covalent binding or through specific interactions. The first protein used in this work was laccase, a copper-containing redox enzyme that catalyse the oxidation of a broad range of polyphenols and aromatic substrates, coupled to the reduction of O2to H2O without need of cofactors. Applications of laccases have been reported in food, pulp, paper, and textile industry, and also in biosensor development. Some uses require the immobilization of the enzyme on solid supports by adsorption, covalent attachment, entrapment, etc, on several substrates. Especially for biosensor development, highly active, stable and reproducible immobilization of laccase is required.

Unlabeled Antibody Immunocytochemistry Applied to Murine Mammary Tumor Cells

1975 ◽  
Vol 33 ◽  
pp. 390-391
Author(s):  
Wm. J. Arnold ◽  
J. Russo ◽  
H. D. Soule ◽  
M. A. Rich
Keyword(s):  
Horseradish Peroxidase ◽  
Mammary Tumor ◽  
Covalent Binding ◽  
Petri Dish ◽  
Gamma Chain ◽  
Mammary Tumor Virus ◽  
Mammary Tumor Cells ◽  
Murine Mammary Tumor ◽  
Tumor Virus ◽  
Unlabeled Antibody

Our studies of mammary tumor virus have included the application of the unlabeled antibody enzyme method of Sternberger to mammary tumor derived mouse cells in culture and observation with an electron microscope. The method avoids the extravagance of covalent binding of indicator molecules (horseradish peroxidase) with precious antibody locator molecules by relying instead upon specific antibody-antigen linkages. Our reagents included: Primary Antibody, rabbit anti-murine mammary tumor virus (MuMTV) which was antiserum 113 AV-2; Secondary Antibody, goat anti-rabbit IgG gamma chain (Cappel Laboratories); andthe Indicator, rabbit anti-horseradish peroxidase - horseradish peroxidase complex (PAP) (Cappel Labs.). Dilutions and washes were made in 0.05 M Tris 0.15 M saline buffered to pH 7.4. Cell monolayers, after light fixation in glutaraldehyde, were incubated in place by a protocol adapted from Sternberger and Graham and Karnovsky, then embedded by our usual method for monolayers. Reagents were confined to specific areas by neoprene 0-rings (Parker Seal Co.) reducing the amount of reagent needed to 50 microliters, 1/6th of that required to wet a 35 mm petri dish.

Common modifications of selenocysteine in selenoproteins

2019 ◽  
Vol 64 (1) ◽  
pp. 45-53 ◽  
Author(s):  
Elias S.J. Arnér
Keyword(s):  
Amino Acids ◽  
Covalent Binding ◽  
Physicochemical Characteristics ◽  
Redox Active

Abstract Selenocysteine (Sec), the sulfur-to-selenium substituted variant of cysteine (Cys), is the defining entity of selenoproteins. These are naturally expressed in many diverse organisms and constitute a unique class of proteins. As a result of the physicochemical characteristics of selenium when compared with sulfur, Sec is typically more reactive than Cys while participating in similar reactions, and there are also some qualitative differences in the reactivities between the two amino acids. This minireview discusses the types of modifications of Sec in selenoproteins that have thus far been experimentally validated. These modifications include direct covalent binding through the Se atom of Sec to other chalcogen atoms (S, O and Se) as present in redox active molecular motifs, derivatization of Sec via the direct covalent binding to non-chalcogen elements (Ni, Mb, N, Au and C), and the loss of Se from Sec resulting in formation of dehydroalanine. To understand the nature of these Sec modifications is crucial for an understanding of selenoprotein reactivities in biological, physiological and pathophysiological contexts.

Effect of pomegranate fruit supplementation on performance and various markers in athletes and active subjects: a systematic review

2019 ◽  
pp. 1-15
Author(s):  
Alicja Urbaniak ◽  
Anna Skarpańska-Stejnborn
Keyword(s):  
Vessel Diameter ◽  
Whole Body ◽  
Double Blind Study ◽  
Double Blind ◽  
Physically Active ◽  
Highly Active ◽  
Body Strength ◽  
Rate Of Increase ◽  
Study Designs ◽  
Pomegranate Fruit

Abstract. The aim of the study was to review recent findings on the use of POM supplements in athletes of various disciplines and physically active participants. Eleven articles published between 2010 and 2018 were included, where the total number of investigated subjects was 176. Male participants constituted the majority of the group (n = 155), as compared to females (n = 21). 45% of research described was conducted on athletes, whereas the remaining studies were based on highly active participants. Randomised, crossover, double-blind study designs constituted the majority of the experimental designs used. POM supplementation varied in terms of form (pills/juice), dosage (50 ml–500 ml) and time of intervention (7 days–2 months) between studies. Among the reviewed articles, POM supplementation had an effect on the improvement of the following: whole body strength; feeling of vitality; acute and delayed muscle fatigue and soreness; increase in vessel diameter; blood flow and serum level of TAC; reduction in the rate of increase for HR, SBP, CK and LDH; support in the recovery of post-training CK, LDH, CRP and ASAT to their baseline levels; reduction of MMP2, MMP9, hsCRP and MDA; and increased activity of antioxidant enzymes (glutathione peroxidase and superoxide dismutase). In the majority of reviewed articles POM supplementation had a positive effect on a variety of parameters studied and the authors recommended it as a supplement for athletes and physically active bodies.

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