scholarly journals Protein covalent modification of biologically active quinones

2004 ◽  
Vol 69 (11) ◽  
pp. 901-907 ◽  
Author(s):  
Dusan Sladic ◽  
Irena Novakovic ◽  
Zoran Vujcic ◽  
Tatjana Bozic ◽  
Natasa Bozic ◽  
...  
Keyword(s):  
Antitumor Activity ◽  
Chemical Modification ◽  
Covalent Modification ◽  
Biologically Active ◽  
Amino Groups ◽  
Sds Page ◽  
Protein Covalent

The avarone/avarol quinone/hydroquinone couple shows considerable antitumor activity. In this work, covalent modification of ?-lactoglobulin by avarone and its derivatives as well as by the synthetic steroidal quinone 2,5(10)-estradiene- 1,4,17-trione and its derivatives were studied. The techniques for studying chemical modification of ?-lactoglobulin by quinones were: UV/Vis spectrophotometry, SDS PAGE and isoelectrofocusing. SDS PAGE results suggest that polymerization of the protein occurs. It could be seen that the protein of 18 kD gives the bands of 20 kD, 36 kD, 40 kD, 45 kD, 64 kD and 128 kD depending on modification agent. The shift of the pI of the protein (5.4) upon modification toward lower values (from pI 5.0 to 5.3) indicated that lysine amino groups are the principal site of the reaction of ?-lactoglobulin with the quinones.

scholarly journals Chemical modification of β-lactoglobulin by quinines

2003 ◽  
Vol 68 (4-5) ◽  
pp. 243-248 ◽  
Author(s):  
Irena Novakovic ◽  
Zoran Vujcic ◽  
Tatjana Bozic ◽  
Natasa Bozic ◽  
Nenad Milosavic ◽  
...  
Keyword(s):  
Antitumor Activity ◽  
Chemical Modification ◽  
Model Compound ◽  
Cow Milk ◽  
Amino Groups ◽  
Tert Butyl ◽  
Sds Page ◽  
Covalent Modifications ◽  
Β Lactoglobulin

The avarone/avarol quinone/hydroquinone couple, as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of ?-lactoglobulin, isolated from cow milk, by avarone, its model compound 2-tert-butyl-1,4-benzoquinone, and several of their alkylthio derivatives were studied. The techniques applied for assaying the modifications were UV/VIS spectrophotometry, SDS PAGE and isoelectrofocusing. The results of the SDS PAGE suggest that polymerisation of the protein occurs. The shift of the pI of the protein upon modification toward lower values indicates that lysine amino groups are the principal site of the reaction of ?-lactoglobulin with the quinines.

scholarly journals Comparative Analysis of Electrophoretic Profile of Major Proteins of Milk from Alpine and Carpathian Goats

2017 ◽  
Vol 74 (1) ◽  
pp. 20 ◽  
Author(s):  
Alina NASALEAN ◽  
Laurentiu OGNEAN ◽  
Sergiu MUNTEAN ◽  
Stefana BALICI ◽  
Horea MATEI
Keyword(s):  
Protein Profile ◽  
Milk Proteins ◽  
Goat Milk ◽  
Protein Composition ◽  
Raw Milk ◽  
Biologically Active ◽  
Protein Fractions ◽  
Animal Nutrition ◽  
Sds Page ◽  
Percentage Data

The milk’s proteins provide nutritional and biologically active values, essential in human and animal nutrition. In the case of goat milk, the proteins’ concentration and quality represent basic indices for the evaluation of the nutritional and biologically active values. The proposal is to comparatively analyse the protein profile of milk. The milk was collected from two different breeds: French Alpine and Romanian Carpathian. During March and April 2016 there were collected samples of raw milk in hygienic and sanitation conditions. There were two lots: first lot has 10 Carpathian goats and the second lot has 10 Alpine goats. The protein composition of goat milk was established with SDS-PAGE, after the evaluation of the total proteins’ concentration with the Bradford method. The quantitative and percentage data obtained with electrophoresis revealed few differences between those 8 identified protein fractions. Between those two lots, regarding the levels of β-CN, k-CN and β-lactoglobulines there were significant differences. The other protein fractions have values almost identical. Statistical analysis of obtained data shaped the differences in the protein profile at those two breeds. Based on those differences it is to note the superior potential of the Alpine breed regarding the content in biologically active milk proteins. Regarding the obtained data, this study brings new contributions for the evaluation and analysis of protein profile as a nutritive and biologically active component of goat milk, confirming its character as a functional aliment.

scholarly journals Chemical Modification and Antitumor Activity of Polysaccharides from the Mycelium of Liquid-cultured Grifola frondosa.

1994 ◽  
Vol 41 (10) ◽  
pp. 733-740 ◽  
Author(s):  
Cun ZHUANG ◽  
Takashi MIZUNO ◽  
Hitoshi ITO ◽  
Keishiro SHIMURA
Keyword(s):  
Antitumor Activity ◽  
Chemical Modification ◽  
Grifola Frondosa

scholarly journals INDIVIDUAL HUMAN SERA RESPONSE AGAINST PROTEIN EXTRACTS FROM SALIVARY GLAND OF Aedes aegypti

2015 ◽  
Vol 2 (1) ◽  
pp. 86
Author(s):  
Rike Oktarianti ◽  
Kartika Senjarini ◽  
Fatchiyah . ◽  
Aulani’am .
Keyword(s):  
Salivary Gland ◽  
Aedes Aegypti ◽  
Complex Mixture ◽  
Biologically Active ◽  
Dengue Viruses ◽  
Sds Page ◽  
Human Sera ◽  
Immunogenic Proteins ◽  
Hematophagous Arthropods ◽  
Individual Human

The saliva of hematophagous arthropods contains a complex mixture of biologically active proteins. These proteins may modify hemostatic responses and induce both cellular immunity and the production of specific antibodies, and thus influence the transmission of its pathogens from arthropods vector to human host. Aedes aegypti is the main vector for transmission of dengue viruses into human. The objective of this study was to examine individual human sera response against protein extracts from salivary gland of Ae aegypti that mediate the infection of dengue viruses. We did a cross reaction test of human sera from healthy people in endemic and non-endemic area, and dengue patients againts SGE of Ae. aegypti to distinguish and to identify the immunogenic proteins using Western Blot Analysis. About 15 protein bands of SGE from Ae. aegypti ranging from 15 kDa up to 255 kDa were identified on 12% SDS-PAGE. Seven dominant bands were detected, i.e ~255, 56, 42, 31, 27, 26 and 15 kDa. Two immunogenic proteins, as represented by two bands, i.e. ~31 and 56 kDa were found only in samples from people who were previously exposed to mosquitoes bites, and not in people who had not been exposed. Therefore, these immunogenic salivary proteins may serve as indicators for the immune response in human against protein from salivary gland of Ae. aegypti.Keywords: immunogenic proteins, salivary gland, Aedes aegypti

scholarly journals Chemical modification of the adeno-associated virus capsid to improve gene delivery

2020 ◽  
Vol 11 (4) ◽  
pp. 1122-1131 ◽  
Author(s):  
Mathieu Mével ◽  
Mohammed Bouzelha ◽  
Aurélien Leray ◽  
Simon Pacouret ◽  
Mickael Guilbaud ◽  
...  
Keyword(s):  
Gene Delivery ◽  
Chemical Modification ◽  
Neutralizing Antibodies ◽  
Cell Tropism ◽  
Amino Groups ◽  
Chemical Modifications ◽  
Virus Capsid ◽  
Adeno Associated Virus

Bioconjugated AAV vectors, achieved by coupling of ligands on amino groups of the capsid, are of great interest for gene delivery. Chemical modifications can be used to enhance cell tropism and to decrease interactions with neutralizing antibodies.

scholarly journals Further Characterization of an Interleukin-2-1Ike Cytokine Produced byXenopus LaevisT Lymphocytes

1993 ◽  
Vol 3 (3) ◽  
pp. 231-238 ◽  
Author(s):  
Laura Haynes ◽  
Nicholas Cohen
Keyword(s):  
T Cell ◽  
South African ◽  
Interleukin 2 ◽  
Biological Properties ◽  
Biologically Active ◽  
Lectin Affinity Chromatography ◽  
Sds Page ◽  
Cell Mitogen ◽  
Clawed Frog

A T-cell growth factor (TCGF) is produced by antigen- or mitogen-stimulated T lymphocytes from the South African clawed frogXenopus laevis. This study further defines the physical and biological properties of this cytokine and demonstrates that TCGF is biochemically similar to mammalian interleukin-2 (IL-2). Biologically active TCGF eluted from SDS-PAGE displays a Mrof 16 kD and lectin-affinity chromatography indicates that the three-dimensionmal configuration of carbohydrates on TCGF and human IL-2 is similar. Secretion of TCGF is detectable 1 day after stimulation of splenocytes with the T-cell mitogen phytohemagglutinin (PHA) and peaks following 2 to 3 days of stimulation. Finally, despite the biological and physical similarities betweenXenopusTCGF and mammalian IL-2, anti-human IL-2 monoclonal antibodies do not recognizeXenopusTCGF.

scholarly journals Protein quantification and visualization via ultraviolet-dependent labeling with 2,2,2-trichloroethanol

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Anand Chopra ◽  
William G. Willmore ◽  
Kyle K. Biggar
Keyword(s):  
Light Exposure ◽  
Covalent Modification ◽  
Protein Quantification ◽  
Visible Range ◽  
Uv Absorbance ◽  
Polyacrylamide Gels ◽  
Fluorescent Emission ◽  
Tyrosine Residues ◽  
Sds Page ◽  
Low Volume

Abstract The incorporation of 2,2,2-trichloroethanol in polyacrylamide gels allows for fluorescent visualization of proteins following electrophoresis. Ultraviolet-light exposure, in the presence of this trichlorinated compound, results in a covalent modification of the tryptophan indole ring that shifts the fluorescent emission into the visible range. Based on this principle, we used 2,2,2-trichloroethanol to develop a microplate format protein quantification assay based on the fluorescent signal generated by modified proteins. We also demonstrated a specific fluorescent emission of 2,2,2-trichloroethanol-labeled protein at 450 nm, with a 310 nm excitation, resulting from modification of both tryptophan and tyrosine residues. Following optimization, this protein quantification assay displayed superior sensitivity when compared to UV absorbance at 280 nm (A280), and enabled quantification beyond the linear range permitted by the Bradford method. This 100 μL assay displayed a sensitivity of 10.5 μg in a range up to at least 200 μg. Furthermore, we extended the utility of this method through the development of a 20 μL low-volume assay, with a sensitivity of 8.7 μg tested up to 100 μg, which enabled visualization of proteins following SDS-PAGE. Collectively, these results demonstrate the utility of 2,2,2-trichloroethanol-based protein quantification and demonstrates the protein visualization in polyacrylamide gels based on 2,2,2-trichloroethanol-labeling pre-electrophoresis.

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