Plasma albumin, bovine

Marsh MM. Spectropolarimetric studies on proteins. Bovine plasma albumin and insulin. J Am Chem Soc 1962 84 1896-900. 

Moore, J.F., and Ward, W.H. (1956) Cross-linking of bovine plasma albumin with wool keratin. /. Am. Chem. Soc. 78, 2414. 

FlC. 9. Nonparallel regeneration of the functions for bilirubin binding and fatty acid binding in bovine plasma albumin. The oxidative regeneration of reduced albumin was carried out at protein concentrations of 1 ft,M at 25°C in 0.10 M Tris-chloride buffer, pH 8.0, containing 1 mM EDTA and 1 mM reduced and 0.10 mM oxidized glutathione (Johanson et al, 1977, 1981). 

Fig. 11. Plot of K (ReiReay (in cm. sec. " ) against C, (dynes cm." ) for spread monolayers of bovine plasma albumin. K refers to the over-all mass-transfer coefficient for isopropanol transferring from water to benzene, and various stirring speeds are employed in the apparatus of Fig. 5(b). R refers to the runs using redistilled water, H to those using 0.01 N HCl, N to those using 0.01 NaOH, and T to those using tap water (60).

Kaplan, L. J. and Foster, J. F. 1971. Isoelectric focusing behavior of bovine plasma albumin, mercaptalbumin, and /3-lactoglobulin A and B. Biochemistry 10, 630-636. 

King, T. P. and Spencer, E. M. 1970. Structure studies and organic ligand-binding properties of bovine plasma albumin. J. Biol. Chem. 245, 6134-6148. 

Sogami, M., Nagaoka, S., Itoh, K.B and Sakata, S. 1973. Fluorimetric studies on the structural transition of bovine plasma albumin in acidic solutions. Biochim. Biophys. Acta 310, 118-123. 

Sogami, M. and Ogura, S. 1973. Structural transition in bovine plasma albumin. Location of tyrosyl and tryptophyl residues by solvent perturbation difference spectra. 

Spencer, E. M. 1974. Amino acid sequence of the alanyl peptide from cyanogen bromide cleavage of bovine plasma albumin. Arch. Biochem. Biophys. 165, 80-89. 

Malonaldehyde (MA) is a major end product of oxidizing or rancid lipids and it accumulates in moist foodstuffs (6). Several MA-protein systems have been studied. Chio and Tappel combined RNAase and MA to demonstrate fluorescence attributed to a conjugated imine formed by crosslinking two e-amino groups with the dialdehyde (7). Shin studied the same reaction and found it to be dependent on pH and reactant concentrations (8). Crawford reported the reaction between MA and bovine plasma albumin (BPA) also to be pH dependent, and of first order kinetics with a maximum rate near pH 4.30. At room temperature 50-60% of the e-amino groups were modified—40% in the first eight hours, the remainder over a period of days (9). 

A model system demonstrating the nutritional destruction of lysine in bovine plasma albumin (BPA) by reaction with either a dialdehyde (MA) or a keto-aldehyde (MGA) was studied in relation to reaction rates as affected by pH, temperature, reaction time and carbonyl concentration. The BPA was Fraction V obtained from Schwartz/Mann and had a molecular weight of 69 x 103 with sixty lysine residules/mole, an assayed content of 11.4%. It was dissolved in 0.0200 M phosphate-citrate buffer adjusted to the desired pH. Malonaldehyde was prepared by acid hydrolysis of its bis-(dimethyl acetal). An aqueous solution of pyruvic aldehyde was diluted with distilled water and phosphate-citrate buffer to give an MGA solution of the desired pH (16). 

Figure 4. Rate of lysine loss at various ratios of malonaldehyde and methylglyoxal to bovine plasma albumin.

Chlorophyll studies of adducts with various biological molecules are also known (bovine plasma albumin and (3-carotene [195], quinone riboflavin [196], and NADH [173]. Mitsui et al. [196] have shown that in porphyrin complexes of viologen the counterion (I-, C1-, Br-) affects the electron transfer process by reduction of the electron-accepting properties of viol-... 

Bovine plasma albumin and dog serum albumin have been iodinated with di- I-labeled methyl p-hydroxybenzimidate. The authors did not attempt to obtain maximum specific activity, but rather examined the effect of reaction conditions on the rate of amidination and yield of iodinated product. The set of conditions given above is only one of the many tested. It was chosen because it gave the highest incorporation of I. Overall the results showed that the iodination reaction will proceed at pH 7.5-9.5 and... 

H6. Hartley, R. W., Peterson, E. A., and Sober, H. A., The relation of free sulfhydryl groups to chromatographic heterogeneity and polymerization of bovine plasma albumin. Biochemistry 1, 60-68 (1962). 

Y2. Yang, J. T., and Foster, J. F., Changes in the intrinsic viscosity and optical rotation of bovine plasma albumin associated with acid binding. J. Am. Chem. Soc. 76, 1588-1595 (1954). 

Protein was measured as bovine plasma albumin by the method of Lowry et al. (19). 

Amnion interferon Bovine plasma albumin Sepharose 4B 216... 

Time effects have also been observed for bovine plasma albumin, horse serum albumin and rabbit y-globulin (Beaven and Holiday, 1950). The behavior of bovine plasma albumin was most striking the intensity of the absorption in 0.1 N alkali increased steadily over a period of ca. 3 hours at room temperature the light-scattering properties of the solution, as shown by its apparent absorption on the long-wave side of the absorption band proper, also increased. Of the few proteins which were examined, only lysozyme showed no time effect. With trypsin the change in absorption was small and complete in a few minutes at pH 13, but the solution then became visibly turbid. 

Figure 7. Infrared difference spectra. Top of azidomet-myoglobin vs. metmyoglobin (0.02M). Middle of azidomeU hemoglobin vs. bovine plasma albumin (O.OIM). Bottom of sodium azide in 0.05M citrate buffer (pH 3) vs. buffer.

More detailed information on ion exchange involved in protein adsorption can be derived from titration experiments in systems where the charge of the protein and the sorbent can be varied independently. Currently, we are studying such systems, using bovine plasma albumin (BPA) and cytochrome c as the proteins and silver iodide (Agl) particles as the sorbent. In these systems there are two potential determining ion couples, the H" /oh" couple for the protein and the Ag" "/ " couple for the sorbent. They enable independent control of protein and surface charge. Below, we will briefly discuss some results obtained with the BPA - Agl system. 

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