By Theodore Peters Jr.
The 1st of its sort, All approximately Albumin summarizes the chemistry, genetics, metabolism, medical implications, and advertisement elements of albumin. It offers the main updated sequences, constructions, and compositions of many species, and contains greater than 2000 references.
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Extra resources for All About Albumin: Biochemistry, Genetics, and Medical Applications
Ovalbumin and [3lactoglobulin, for example, exchange deuterium atoms considerably less rapidly. , 1985). Like other proteins, components of albumin are also constantly moving on more rapid time scales. Gurd and Rothgeb (1979) have reviewed these motions. Reorientation of amino acid side chains occurs in 10-10-10-11 s, and ionizations in 10- I I s. Amino acid side chains not restricted by 7r bonding rotate about their single bonds; a methyl group rotates in 5 • 10-12 s. , 1979), rotates independently at a rapid rate, about 10-l0 s rotational correlation time.
Bloomfield (1966) proposed such a model from hydrodynamic studies without knowledge of Fig. 2-5. Model of the HSA molecule derived from hydrodynamic studies. II. Tertiary Structure and Physical Chemical Behavior 27 the homologous domains; he showed three spheres in a row, with diameters of 38, 53, and 38 A rather than of equal size. 2. 9; at neutral pH no structure could be defned, an implication that the domains separate reversibly under acid conditions. 4. They favored a more spherical shape for BSA.
1971), and the review by Foster (1960), to which the reader interested in the development of equations from Debye-H~ickel theory is referred. The titration curve is flattest between pH 5 and pH 8, so that albumin is a rather weak buffer in the physiological pH range. Here it is mainly the imidazoles of the histidines and the terminal amino and carboxyl groups that are being protonated. The net charge is also affected slightly in this range by calcium binding. Figge et al. , 1989b), and showed that it closely agreed with the curve obtained by titration.