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Biomedical subjects

H B Bohidar

Publications and source records attributed to H B Bohidar.

22 records · Page 2Linked to original sources
PubMed1991

Heat aggregation studies of phycobilisomes, ferritin, insulin, and immunoglobulin by dynamic light scattering.

Dynamic laser light scattering studies on the heat aggregation behavior of phycobilisomes (PBS), ferritin, insulin, and immunoglobulin (IgG) in dilute aqueous solutions has been reported. Except for PBS, results are reported for heat aggregation trends in these proteins for three different pH environments (4.0, 7.5, 9.1). For PBS, studies were performed only in the neutral buffer medium (pH 7.5). The experiments were performed in the very dilute concentration regime (between 0.23 and 1.8 gL-1). For all these samples heat aggregation and dissociation trends were found to be linear with temperature. Upon temperature reversal (self-cooling), hysteresis-like behavior observed in insulin was found to be predominantly large at pH 7.5. PBS, ferritin, and IgG showed no such behavior at any of three pH values, and retraced their path of aggregation while dissociating on temperature reversal. Heat aggregation and dissociation processes in ferritin were found to be independent of pH. The IgG samples showed smooth aggregation tendency only up to 35 degrees C in the buffer media pH 4.0 and 9.1, whereas for pH 7.0 the same could be observed until 60 degrees C. Low polydispersity in the correlation spectra was observed in case of all these samples.

Ferritins↗
PubMedDate not supplied

Systematic of alcohol-induced simple coacervation in aqueous gelatin solutions.

Turbidity measurements performed at 450 nm were used to follow the process of simple coacervation when 1% (w/v) aqueous alkali processed gelatin (type-B) solutions were titrated with methanol, ethanol, propanol, and tert-butyl alcohol at various pHs of the solution ranging from pH = 5 to 8 and ionic strengths varying from I = 0.01 to 0.1 M NaCl. The titration profiles clearly established the transition points in terms of the percentage of volume of alcohol added relative to that of solvent corresponding to the first occurrence of turbidity (Vt) and a point of turbidity maximum (Vp). Addition of more alcohol drove the system toward precipitation. The values of Vt and Vp characterized the initiation of intramolecular folding and intermolecular aggregate formation of the charge neutralized gelatin molecules and the subsequent micro coacervate droplet formation. The state of intermolecular aggregates and that of folded gelatin molecules could be characterized by dynamic laser light scattering experiments, which implied spontaneous segregation of particle sizes preceding coacervation. The aggregates constitute the coacervate phase while the folded gelatin molecules mostly stay dispersed in the supernatant. The data taken together reveal the role played by solution entropy in addition to that of electrostatic and solute-solvent interactions, which had been overlooked hitherto.

Alcohols↗
PubMedDate not supplied

Flory temperature and upper critical solution temperature of gelatin solutions.

The Flory temperatures (theta) measured by turbidity experiments performed on gelatin solutions were found to be 12 +/- 0.3, 13 +/- 0.3, 14 +/- 0.3, 14.5 +/- 0.3, and 15 +/- 0.3 degrees C for salt concentrations 0.1, 0.075, 0.05, 0.025, and 0 M (NaCl), respectively. Estimated persistence length (l(p)) of this weakly charged polyelectrolyte could be deduced from the Benoit and Doty (J. Phys. Chem. 1953, 57, 958) relationship with the approximation that this biopolymer assumes a compact near-globular shape at Flory temperature, implying l(p) = 9(R(h))(2)/(5L(m)), where L(m) is the contour length and R(h) is the hydrodynamic radius. It was found that l(p) approximately 2.2 +/- 0.2 nm at room temperature (20 degrees C), invariant of salt concentration. The Flory expansion factor (alpha= R(h)(T)/R(h)(theta) = 1.5+/-0.2) was found to be almost constant. theta-Composition for this biopolymer was deduced from turbidimitric titration of aqueous gelatin solutions with the alcohols methanol, ethanol, 2-propanol, and tert-butyl alcohol. It appears that hydrophobic interactions play a crucial role in causing chain collapse at theta-temperature and composition.

Gelatin↗