S Gurnani

ORCID: 0009-0008-0655-094X
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About
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Research Areas
  • Enzyme Structure and Function
  • Enzyme Production and Characterization
  • Protein Interaction Studies and Fluorescence Analysis
  • Protein Structure and Dynamics
  • Biochemical and Molecular Research
  • Glycosylation and Glycoproteins Research
  • Lipid Membrane Structure and Behavior
  • bioluminescence and chemiluminescence research
  • Analytical Chemistry and Chromatography
  • Neonatal Health and Biochemistry
  • Chemical Synthesis and Analysis
  • Muscle metabolism and nutrition
  • Porphyrin Metabolism and Disorders
  • Cancer Research and Treatments
  • Click Chemistry and Applications
  • Carbohydrate Chemistry and Synthesis
  • Protein purification and stability
  • Aldose Reductase and Taurine
  • Microtubule and mitosis dynamics
  • Thermodynamic properties of mixtures
  • Proteins in Food Systems
  • Biochemical effects in animals
  • Diffusion and Search Dynamics
  • Cancer Treatment and Pharmacology
  • Peptidase Inhibition and Analysis

Boston Medical Center
2025

Acorn
2024

Bhabha Atomic Research Centre
1972-1987

University of Washington
1981

Balfour Beatty (United Kingdom)
1972

Government of India
1955

Abstract— A study has been made of the effects eight amino acids and a group compounds related to tryptophan upon photofading methylene blue under anaerobic conditions excited species generated by flash photolysis dye. These are discussed in relation ease sensitized photooxidation blue, order test hydrogen‐abstraction mechanism proposed for this reaction. In general, susceptible oxidation also act as reducing agents photoreduction while insensitive do not reduce light‐excited dye molecule....

10.1111/j.1751-1097.1972.tb07341.x article EN Photochemistry and Photobiology 1972-08-01

10.1016/0584-8539(83)80007-5 article EN Spectrochimica Acta Part A Molecular Spectroscopy 1983-01-01

Abstract Spectrophotometric techniques have been employed to study the binding of bromophenol red (BPR) hen egg white lysozyme and consequent inhibition enzyme activity. Experimental evidence is given from dye studies in presence hexasaccharide on activity that BPR binds at a site outside proposed cleft region (A–F) such way it inhibits lytic towards cell walls but does not inhibit hexasaccharide. These observations are consistent with kinetics [studied using temperature‐jump (T‐jump)] Co ++...

10.1002/bip.1979.360180809 article EN Biopolymers 1979-08-01

Role of lysine residues in the colchicine binding site and assembly-disassembly process was examined. It observed that at 4 degrees C (pH 7.5-8, 8 +/- 1) N-terminal methionine residue tubulin were all buried within molecule. Evidence indicates epsilon-amino groups are shared by both polymerisation process.

10.1016/0014-5793(83)80491-8 article EN FEBS Letters 1983-02-07

10.1016/0006-291x(83)90390-x article EN Biochemical and Biophysical Research Communications 1983-10-01

Abstract We have carried out DSC investigations of the ice-water [iw, wi and (wi)1], chain-melting (CM) chain ordering (CO) transitions in DPPC-water (model membrane) systems for a range water concentrations both pure DDS-doped samples. The temperatures, T CM co, are hardly affected by inclusion DDS, showing that DDS does not get embedded acyl layers. Increase CO transition widths indicates varied environments DPPC molecules presence DDS. enthalpies point to fact (a) reduces “free” content...

10.1080/00268948308073471 article EN Molecular crystals and liquid crystals 1983-09-01

Multiple forms of lysozyme found in the rat liver were isolated and characterized from cellular organelles. Isolation enzymes was achieved by Sephadex gel filtration chromatography on CM cellulose-column. The purity preparations examined electrophoresis polyacrylamide gel. nuclear moved as a single band indicating homogeneity, whereas other subcellular lysozymes appeared heterogeneous due to presence more than one band, thus showing partial purity. Although similar with respect enzymatic...

10.1271/bbb1961.45.1817 article EN Agricultural and Biological Chemistry 1981-01-01

Abstract The interaction of tylophorinidine (TPD) with lysozyme—a model protein—with biological activity, was investigated by determining its fluorescence and assessing activity under various conditions. results indicated that TPD associated lysozyme at p H 9.2 efficiently an association constant K a 3.3 X 10 4 M –1 26°C. increased the increasing temperature in range 26 to 55°C; calculated enthalpy change Δ found be 2.3 kcal/mol. Under same conditions as above also free amino acid tryptophan...

10.1002/qua.560200224 article EN International Journal of Quantum Chemistry 1981-08-01
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