All About Albumin: Biochemistry, Genetics, and Medical by Theodore Peters Jr.

By Theodore Peters Jr.

The 1st of its style, All approximately Albumin summarizes the chemistry, genetics, metabolism, medical implications, and advertisement elements of albumin. It offers the main updated sequences, buildings, and compositions of many species, and contains greater than 2000 references.

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Extra info for All About Albumin: Biochemistry, Genetics, and Medical Applications

Example text

15 105 cm2 v - I s - ! 1 6828 17 aKey to references (superscript numbers): (1) Charlwood (1961), (2) Squire et ai. (196B8), (3) Hirayama et al. (1990), (4) Oncley et al. (1946), (5) Wagner and Scheraga (1956), (6) Hunter (1966), (7) McMillan (1974), (8) Hughes (1954), (9) Wright and Thompson (1975), (10) He and Carter (1992), (11) Cannistraro and Sacchette (1986), (12) Anderegg et al. (1955), (13) Riddiford and Jennings (1966), (14) Carter and Ho (1994), (15) Creeth (1952), (16) Foster (1960), (17) Longsworth and Jacobsen (1949), (18) Gianazza et al.

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. Hence, although albumin in solution can be considered as having a single shape overall, it is probably more realistic to regard it as an assembly of squirmy, resilient parts, frequently changing in conformation through opening and closing of major crevices.

Albumin Molecule: Structure and Chemistry I0 I0, l 2 2[b"] I~i ~ I t~ I~1 ['~6 T ~ 4 F b 6 P I 8 II I0 IA IB IIA IlIA lib ~ I IIIB I II. Tertiary Structure and Physical Chemical Behavior 35 apparently becomes more compact, the molecule resists proteolytic degradation and heat denaturation, the dielectric constant falls, and bilirubin binding is enhanced. It remains to be seen whether LCFA-induced conformational changes affect the configuration seen in albumin crystals, and whether the structure in a crystal is the same as that in solutiofi.

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