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Scrum albumin

R. A. Thompson, S. Allenmark, The Effect of Long-Chain Alkyl Betainates on the Ar-ylesterase-Like Activity of Bovine Scrum Albumin , llioorg. Chem. 1992, 20, 356-365. [Pg.428]

The order of elution would therefore be catalase, scrum albumin, chymotrypsinogen, myoglobin, and cytochrome c. [Pg.78]

Carraro E, Gasparini S, Petrini T, et al. 1997. Immune response prevalence to formaldehyde-human scrum albumin molecular adduct in a health population. J Environ Pathol Toxicol Oncol 16 215-218. [Pg.374]

Dykewicz MS, Patterson R, Cugell DW, et al. 1991. Serum IgE and IgG to formaldehyde-human scrum albumin Lack of relation to gaseous formaldehyde exposure and symptoms. J Allergy Clin Immunol 87 48-57. [Pg.382]

Disease factors Plasma BChE activity may be reduced in liver cirrhosis, hepatic parenchymal disease, protein malnutrition, low scrum albumin, myocardial infarction, and dermatomyositis (Balistreri and Rej, 1994 Duncan and Griffith, 1992 Vorhaus and Kark, 1953). [Pg.577]

Means, G. E., and Wu, H. L. (1979), The reactive tyrosine residue of human scrum albumin Characierization of its reaction with diisopropylfluorophosphate. Arch. Biochem. Biophys. 194,526-530. [Pg.710]

Sakurai, Y., Ma, S. F., Watanabe, H., Yamaotsu, N., Hirono, S., Kurono, Y., Kragh-Hansen, U and Otagiri, M. (2004). E,siera.se-like activity of scrum albumin Characicrizaiion of its structural chemistry using p-niirophenyl esters a.s. substrates. Phann. Res. 21,285-292. [Pg.710]

Figure 3.28 di lays fluorescence emissicm spectra of Qiun-2 in presence of increased concentrations of human scrum albumin. We can notice that the fluorescence inlensil> of the probe increases accompanied with a of the emis n maximum to short wavelengths. The fluorescence intensi increase indicates that the probe binds to human serum albumin and the blue shift reveals the hydrophobic nature of the landing site compared to free fluorophore in solution. [Pg.125]

Fig. 10. Transient response of the phosphorescence intensity of bovine scrum albumin monitored at 414 nm to a microwave fast-passage magnetic resonance transition which occurs at / = 0. The magnetic resonance, which is centered at 1.657 GHz is due to the tryptophan Tz Tx transition (see Fig. 8). The temperature is 1.3 K, no external magnetic field is present, the solvent is 50% ethylene glycol-water, and the sample is continuously optically pumped. The transient decays os a single exponential since only Tj, is radiative. If both and T had been radiative, a response such as shown in Fig. 1 of Winscom and Maki 8) would have been observed. (From Zuclich et al. lOOh)... Fig. 10. Transient response of the phosphorescence intensity of bovine scrum albumin monitored at 414 nm to a microwave fast-passage magnetic resonance transition which occurs at / = 0. The magnetic resonance, which is centered at 1.657 GHz is due to the tryptophan Tz Tx transition (see Fig. 8). The temperature is 1.3 K, no external magnetic field is present, the solvent is 50% ethylene glycol-water, and the sample is continuously optically pumped. The transient decays os a single exponential since only Tj, is radiative. If both and T had been radiative, a response such as shown in Fig. 1 of Winscom and Maki 8) would have been observed. (From Zuclich et al. lOOh)...
Hluent 0.5 M acetic acid containing 29r isopropanol and 1% bovine scrum albumin (BSA), pH 3.50 Development distance 6.5 cm Development time 2 h... [Pg.644]

Eluent 6% bovine scrum albumin (BSA) in 0.05 M sodium tetraborate contg. 6% isopropanol, pH 9.30 Eluent 6% bovine serum albumin (BSA) in 0.05 M sodium bicarbonate + 0.05 sodium carbonate containing 6% isopropanol. pH 9.80... [Pg.644]


See other pages where Scrum albumin is mentioned: [Pg.251]    [Pg.174]    [Pg.132]    [Pg.152]    [Pg.422]    [Pg.545]    [Pg.845]    [Pg.256]    [Pg.175]    [Pg.433]    [Pg.479]    [Pg.638]    [Pg.659]    [Pg.33]    [Pg.180]    [Pg.63]    [Pg.392]    [Pg.394]    [Pg.410]    [Pg.274]    [Pg.52]    [Pg.247]    [Pg.71]    [Pg.70]   
See also in sourсe #XX -- [ Pg.548 ]




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