By Theodore Peters Jr.
The 1st of its type, All approximately Albumin summarizes the chemistry, genetics, metabolism, medical implications, and advertisement features of albumin. It offers the main updated sequences, buildings, and compositions of many species, and comprises greater than 2000 references.
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Extra info for All About Albumin: Biochemistry, Genetics, and Medical Applications
Fluorescence. Fluorescence, the immediate emission of light on radiation with monochromatic light, is largely attributed to the tryptophans of albumins. 42 2. Albumin Molecule: Structure and Chemistry There is only a minor contribution by the more numerous tyrosines, and that is dependent on the wavelength of the exciting light. When this wavelength is between 295 and 305 nm, tyrosines are not excited, and only a pure tryptophan emission spectrum, centered near 345 nm, is seen. , 1971). Most studies are concerned with the tryptophan fluorescence, and use excitation at ->296 nm.
1967b) explored the initial fragmentation of albumin with trypsin, and showed that a pH near 9 favors the formation of larger fragments than does pH 7-8. 8 and 0 ~ to isolate loops 4-9 of bovine albumin. , 1988a), including one constituting domain III (loops 7-9) prepared by digesting BSA heavily with trypsin while it was bound to a palmitoyl-agarose column. Lapresle and his group at the Institut Pasteur in Paris showed following tryptic cleavage that their antigenic "inhibitor" prepared using a heterogeneous spleen cathepsin equaled loop 9 (Bellon and Lapresle, 1975).
The helical motifs of the six subdomains within the three domains are related by a pseudo twofold axis, with angles of 168 ~ 163 ~ and 171 ~ for domains I-III, respectively (Carter and Ho, 1994). 60 A for 57 atom pairs of domains I, II, and III, respectively. 8 A. He and Carter found the helical bundles of subdomains IIA and IliA to form binding cavities for a number of aromatic small molecules. 98 A. The binding regions are discussed later in Chapter 3. The particular amino acid residues that they place, in the ligand pockets are listed in Table 2-5 and are indicated in Fig.
All About Albumin: Biochemistry, Genetics, and Medical Applications by Theodore Peters Jr.