Bovine optical absorption

Cryoreduced mitochondrial cytochrome c oxidases from bovine heart47 and from the rat heart49 have been characterized by optical absorption spectroscopy. Spectra of the nonequilibrium reduced forms of these enzymes at 77K were red shifted with respect to the spectra measured for the reduced proteins in equilibrium, independent of the presence of cytochrome c or cytochrome a3. 

Fig. 7. A Structural representation of Cu-Zn superoxide dismutase (SOD) active site (from Ref. 31c). B X-band (left) (77K v = 9.2 GHz) (from Ref. 25) and Q-band (right) (173 K v = 35 GHz) (from Ref. 26) EPR spectra of bovine Cu-Zn SOD. C Optical absorption spectra of native...

Fig. 8.1 Optical absorption spectra of aqueous solutions of a nucleic acid (calf thymus DNA) and a protein (bovine serum albumin), both recorded at a concentration of 1.97x10 g L" Adapted from Harm [12] with permission from Cambridge University Press.

FigureS.e Optical absorption spectra of DNA and bovine serum albumin in aqueous solution c= 1.97 X lO grY Adapted with permission from Ref. [9] 1980, Cambridge University Press.

Fig. 4. (A) Normalized absorption (solid line) and fluorescence emission (dotted line) spectrum of diglucamide indotricarbocyanine 4 in bovine plasma (concentration 2 pmol/L ) (B) fluorescence image of a tumor-bearing rat (MTLn-3 mammary carcinoma) in anterior view at 0 h and (C) 24 h after administration of 4 (dose 2 pmol/kg body weight), excitation wavelength 740 nm, detection bandpass 750 - 800 nm [45], Copyright 2001 International Society for Optical Engineering (SPIE)...

Morrissey 53) used transmission infrared spectroscopy to study protein adsorption onto silica particles in a heavy water (DzO) buffer. By observing the shift in the amide I absorption band, he could deduce the fraction of protein carbonyl groups involved in bonding to the silica surface. He found that bovine IgG had a bound fraction of 0.20 at low bulk solution concentrations, but only about 0.02 at high solution concentrations. However, neither prothrombin nor bovine serum albumin exhibited a change in bound fraction with concentration. Parallel experiments with flat silica plates using ellipsometry showed that the IgG-adsorbed layers had an optical thickness of 140 A and a surface concentration of 1.7 mg/m2 at low bulk solution concentration — in concentrated solutions the surface amount was 3.4 mg/m2 with a thickness of 320 A (Fig. 17). 

Figure 7. Laser-induced absorbance changes at 561 nm as a function of time in detergent solubilised bovine rhodopsin (X) and isorhodopsin (9) at room temperature. Bathorhodopsin is the only intermediate during the bleaching of bovine rhodopsin known to absorb strongly at 561 nm. The energy of the 530-nm pump pulse was about 10 4J the energy of the 561-nm probe pulse was about 10 7J. The beam sizes were about 1 mm2 for the pump and 0.5 mm2 for the probe. The samples (about 1.5 mL) were held in 0.5-cm cuvettes. The concentrations were about 4 A cm I at the absorption peaks near 500 nm the ratios A Ajjj were about 0.3 and ratios ASsa. As<)o were about 0.7 for rhodopsin and 0.5 for isorhodopsin. Each data point shown is the average of six (rhodopsin) and nine (isorhodopsin) laser shots. Typical mean standard deviations are 0.03. The zero time is located using a 0.5 cm CS2 Kerr optical shutter at the sample site. The half width at half maximum for the CS2 shutter prompt response curve is about 6 ps.

Fig. 26. The polypeptide backbone absorption region optical activity of two 2Fe 2S proteins (299). The ultraviolet ORD (A) and CD (B) spectra of bovine adrenodoxin (—) and spinach ferredoxin (—), taken in aqueous solutions, pH 7.4...

Figure 23. Time-resolved absorption changes in bovine COX induced by reaction with pulse-radioIyticaUy produced 1-MNA radicals, (a) Bimolecular Cua reduction (fast time scale) and intramolecular reoxidation (slow time scale) monitored at 830 nnL Enzyme concentration 41 pM 1-MNA concentration 5 mM. Buffer 5 roM phosphate 0.25% TWeen20 Argon saturated. pH 7.4. Temperature 298 K. Optical path length 12.3 cm. Pulse width 0.75 ps. (b) Heme-a reduction (both time scales) at 605 nno. Enzyme concentration 15 pAf 1-MNA concentration 5 mM. Buffer 5 mM phosphate 0.25% Tween20 Argon saturated. pH 7.4. Temperature 298 K. Optical path length 3.1 cnL Pulse width 0.2 ps. Time is in seconds the left panel shows the faster phase, while the right one shows the reaction taking place at the slower time scale. The lower panels show residuals of the fits to the data.

Figure 22.8 Absorption spectra of (a) 80 nM of polymer 11 (on a monomer basis) in 20 mM sodium phosphate, pH 7.0, (b) in 20 mM sodium phosphate pH 7.0 with 5.0 icM of native bovine insulin (nBI) and (c) in 20 mM sodium phosphate, pH 7.0, with 5.0 fx.M of amyloid fibrils of bovine insulin (fBI). The inset shows the microtiter plate wells containing polymer 3-nBI (left) and polymer 3 fBI (right). Reprinted with permission from K. P. R. Nilsson, A. Herland, P. Hammarstrom and O. Inganas, Conjugated poly electrolytes conformation-sensitive optical probes for detection of amyloid fibril formation. Biochemistry, 44, 3718-3724 (2005). Copyright 2005 American Chemical Society...

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