A5030830495- Microtubule and mitosis dynamics
- Carbohydrate Chemistry and Synthesis
- Metal complexes synthesis and properties
- Protein Interaction Studies and Fluorescence Analysis
- Synthesis and biological activity
- 14-3-3 protein interactions
- Crystal structures of chemical compounds
- Cancer Treatment and Pharmacology
- Photosynthetic Processes and Mechanisms
- Catalytic Cross-Coupling Reactions
- Lipid Membrane Structure and Behavior
- X-ray Diffraction in Crystallography
- Glycosylation and Glycoproteins Research
- Protein Structure and Dynamics
- Advanced Photocatalysis Techniques
- Crystallization and Solubility Studies
- Synthesis and Characterization of Heterocyclic Compounds
- Hemoglobin structure and function
- Click Chemistry and Applications
- Chemical Synthesis and Analysis
- Gas Sensing Nanomaterials and Sensors
- Fungal Plant Pathogen Control
- Metal-Organic Frameworks: Synthesis and Applications
- Quinazolinone synthesis and applications
- Synthesis of Organic Compounds
Qatar University
2022-2024
Tezpur University
2017-2021
Bose Institute
1984-2007
Visva-Bharati University
2000
Indian Institute of Management Calcutta
1989
National Institute of Diabetes and Digestive and Kidney Diseases
1985-1986
National Institutes of Health
1974-1986
Institute of Art
1985
National Institute of Arthritis and Musculoskeletal and Skin Diseases
1974-1984
University of Kalyani
1979
The binding of [3H]podophyllotoxin to tubulin, measured by a DEAE-cellulose filter paper method, occurs with an affinity constant 1.8 X 10(6) M-1 (37 degrees at pH 6.7). Like colchicine, approximately 0.8 mol podophyllotixin are bound per tubulin dimer, and the reaction is entropy-driven (43 cal deg-1 mol-1). At 37 association rate for podophyllotoxin 3.8 h-1, approximtaely 10 times higher than colchicine; this reflected in activation energies which 14.7 kcal/mol 20.3 colchicine....
Brain and thyroid tissue contain membrane-bound colchicine-binding activity that is not due to contamination by loosely bound cytoplasmic tubulin. This can be solubilized the extent of 80 90% treatment with 0.2% Nonidet P-40 retention colchicine binding. Extracts so obtained a prominent protein band in disc gel electrophoresis co-migrates Membranes, therefrom, exhibit ligand binding properties like tubulin; for KA approximately 1 X 10(6) M-1 brain 0.6 thyroid; vinblastine 8 both tissues;...
Colchicine, which does not fluoresce in aqueous media and organic solvents, exhibits marked fluorescence on combination with brain tubulin, a corrected excitation maximum at 362 nm, an emission 435 quantum yield of about 0.03. From measurements it was found that rat tubulin binds 0.83 moles colchicine per dimer (molecular weight 110,000) association constant 3.2 muM(-1) pH 7.0 37 degrees . These results are excellent agreement those obtained the binding [(3)H]-colchicine. The enthalpy is 10...
Cleavage of tubulin by subtilisin removes a small (Mr less than 2000) fragment from the C-terminal end both alpha and beta subunits. The resulting protein is much reduced in negative charge. cleaved, acidic retains its competence to polymerize GTP-dependent cold-, GDP-, podophyllotoxin-sensitive manner assembles into sheets or bundles twisted filaments. critical concentration for polymerization cleaved about 50-fold lower that intact tubulin. It proposed C termini subunits normally impede...
Limited proteolysis of rat brain tubulin (ab) by subtilisin cleaves a 1-2-kDa fragment from the carboxylterminal ends both CY and / 3 subunits with corresponding loss in negative charge proteins.The fl subunit is split much more rapidly (and exclusively at 5 "C), yielding protein cleaved B intact subunit, called a&, which intermediate charge.Further carboxyl terminus leading, irreversibly, to doubly product, named S, composition a&.Both cleavage products are polymerization-competent their...
Rat brain tubulin possesses two distinct binding sites for vinblastine per molecule: a high-affinity site with an affinity constant of 6.2 x 10(6) M-1 and low-affinity 8 10(4) M-1. The is labile, t1/237 degrees 3.5 hr, protected by colchicine, unaffected salt, whereas the stable but inhibited salt. Binding to both rapid. (6.2 M-1) corresponds half-maximal concentration needed prevent polymerization in vitro, (8 required aggregate tubulin. We conclude that high- sites, respectively, accounts...
The chemical specificity of the colchicine-binding site tubulin is less stringent for presence Bring than Aand C-rings colchicine.Colchicine analogues with modifications in B-ring bind to at same as colchicine.Analogues smaller or no substituents remarkably faster colchicine.Thus, a compound without [2-methoxy-5-(2',3',4'-trimethoxyphenyl)tropone] binds even 4 "C and
Colchicine fluoresces when bound to tubulin but not in water, dioxane, or benzene. The basis of the fluorescence has now been investigated. higher alcohols and shows a blue shift as function chain length. Glycerol produces efficiency further shift. Plots 1/fluorescence versus T/eta yield straight lines for both glycerol/water mixtures. Fluorescence glycerol/dimethyl sulfoxide mixtures, which dielectric constant remains unchanged, varies solvent viscosity. Even highly nonpolar solvents such...
Several properties of the colchicine-tubulin interaction such as association rate, reversibility, and promotion drug fluorescence have been related to B ring colchicine. The itself retards binding substitution at C-7 leads further rate decreases that appear be both substituent bulk presence a N-acyl group. Thus, decreasing order rates is 2-methoxy-5-(2',3',4'-trimethoxyphenyl)tropone greater than deacetamidocolchicine deacetylcolchicine or equal colcemid colchicine...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThyroid tubulin, purification and propertiesB. Bhattacharyya J. WolffCite this: Biochemistry 1974, 13, 11, 2364–2369Publication Date (Print):May 1, 1974Publication History Published online1 May 2002Published inissue 1 1974https://pubs.acs.org/doi/10.1021/bi00708a020https://doi.org/10.1021/bi00708a020research-articleACS PublicationsRequest reuse permissionsArticle Views48Altmetric-Citations33LEARN ABOUT THESE METRICSArticle Views are the...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAnion-induced increases in the rate of colchicine binding to tubulinB. Bhattacharyya and J. WolffCite this: Biochemistry 1976, 15, 11, 2283–2288Publication Date (Print):June 1, 1976Publication History Published online1 May 2002Published inissue 1 June 1976https://pubs.acs.org/doi/10.1021/bi00656a006https://doi.org/10.1021/bi00656a006research-articleACS PublicationsRequest reuse permissionsArticle Views42Altmetric-Citations30LEARN ABOUT THESE...
Simple, portable, and low-cost paper-based sensors are alternative devices that have the potential to replace high-cost sensing technologies. The compatibility of paper base biosensors for both chemical biochemical accentuates its feasibility application in clinical diagnosis, environmental monitoring, food quality monitoring. High concentration copper blood serum urine is associated with diseases like liver diseases, carcinomas, acute chronic infections, rheumatoid arthritis, etc. Detection...
Abstract Electrochemical water splitting is a promising pathway for effective hydrogen (H 2 ) evolution in energy conversion and storage, with electrocatalysis playing key role. Developing efficient, cost-effective stable catalysts or electrocatalysts critical from splitting. Herein, we evaluated graphene-modified nanoparticle catalyst reaction (HER). The electrocatalytic H production rate of reduced graphene oxide-titanium oxide-nickel oxide-zinc oxide (rGO–TiO –NiO–ZnO) high exceeds that...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTLocal Unfolding and the Stepwise Loss of Functional Properties TubulinDan L. Sackett, B. Bhattacharyya, J. WolffCite this: Biochemistry 1994, 33, 43, 12868–12878Publication Date (Print):January 1, 1994Publication History Published online1 May 2002Published inissue 1 January 1994https://pubs.acs.org/doi/10.1021/bi00209a019https://doi.org/10.1021/bi00209a019research-articleACS PublicationsRequest reuse permissionsArticle...
4,4'-bis(1-anilino-8-naphthalenesulfonic acid (Bis-ANS), an environment-sensitive fluorescent probe for hydrophobic region of proteins, binds specifically to the C-terminal domain lambda repressor. The binding is characterized by positive cooperativity, magnitude which dependent on protein concentration in range where dimeric repressor aggregates a tetramer. In this range, cooperativity becomes more pronounced at higher concentrations. This suggests preferential Bis-ANS form Binding single...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThe carboxy terminus of the .alpha. subunit tubulin regulates its interaction with colchicineKrishnendu Mukhopadhyay, Pradip K. Parrack, and B. BhattacharyyaCite this: Biochemistry 1990, 29, 6845–6850Publication Date (Print):July 24, 1990Publication History Published online1 May 2002Published inissue 24 July 1990https://pubs.acs.org/doi/10.1021/bi00481a013https://doi.org/10.1021/bi00481a013research-articleACS PublicationsRequest reuse...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTReversible dimer dissociation of tubulin S and detected by fluorescence anisotropyDulal Panda, Siddhartha Roy, B. BhattacharyyaCite this: Biochemistry 1992, 31, 40, 9709–9716Publication Date (Print):October 13, 1992Publication History Published online1 May 2002Published inissue 13 October 1992https://pubs.acs.org/doi/10.1021/bi00155a026https://doi.org/10.1021/bi00155a026research-articleACS PublicationsRequest reuse permissionsArticle...