By Donald M. Kirschenbaum
After you have visible the spectrum of 1 protein you may have obvious the spectra of all professional teins. Or so it should look. whereas the final features of the absorption curve might sound to be related for all proteins (i. e. , in acid and impartial resolution there's a minimal at 250 nm, a greatest at 278-282 nm, and no absorption above 310 nm; in alkaline resolution the utmost and minimal shift to longer wavelengths), there are sophisticated changes that are noticeable while the spectra of many proteins are in comparison. it's those variations which replicate adjustments in amino acid content material and within the milieu during which the protein has been dissolved. The spectra during this booklet offer samples of those refined spectral variations and allow comparisons to be made. This ebook was once ready to have its index learn and its contents said. For the reader who wants to comprehend what a protein spectrum feels like in acid and alkaline media, after X-ray or UV irradiation, or after photo-oxidation or B-bromosuccinimide remedy, spectral representations of a majority of these experimental occasions and so forth can be found. The indicies have been ready to supply the utmost info with the minimal attempt. as well as an alphabetical directory, all spectra are observed by means of species, tissues, and the organs from which they have been taken. There also are "environmental" indicies concerning the remedy the proteins acquired sooner than having their spectra taken. Technical info pertaining to instrumentation is missing.
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Additional resources for Atlas of Protein Spectra in the Ultraviolet and Visible Regions
000075 M with respect to FAD. Holoenzyme. 001 M oc-butenoate. NAME: D-Amino Acid Oxidase SOURCE: pi S kidney REFERENCE: C. V. F. Kalse, A. F. Koster, Biochim. Biophys. Acta Library, 8_ (1966). 3 PH D-Am'ino Acid Oxidase. After addition of 10 mM sodium phenobarbital. NAME: D-Amino Acid Oxidase SOURCE: Pig kidney REFERENCE: C. V. F. Kalse, A. F. Koster, Biochim. Biophys. Acta Library, <3, 2^2 (1966). FAD. FAD. FAD. NAME: D-Amino Acid Oxidase SOURCE: pig kidney REFERENCE: K, Yagi, Biochim. Acta Library, 8_, 210 (1966).
002 M DL-pipecolate. Curve I : Purple complex. Curve II : After 20 hours illumination. Curve III : After ko hours illumination. NAME: D-Amino Acid Oxidase SOURCE: pig kidney REFERENCE: v. Massey, G. Palmer and R. Bennet, Biochim. Biophys. Acta, U8, 1 (1961). 3. Upper curve: Enzyme. Lower curve: Enzyme + 900 moles DL-alanine. NAME: D-Amino Acid Oxidase SOURCE: Pig kidney REFERENCE: K, Yagi and N. , Tokyo, 67, 599 (1970). 3. D-Amino acid oxidase mixed anaerobically •with D-proline in the presence of A'pyroline 2-carboxylate, Curve I : Purple complex.
H . Sands, Biochim. Biophys. Library, 8_, 133 (1966). 1 M pyrophosphate, pH 8 . 17 moles piperidine 2-carboxylate. 17 moles D-pipecolic acid. 35 moles D-pipecolic acid. Curve k: + 52 moles D-pipecolic acid. Anaerobic conditions at 170C. NAME: D-Amino Acid Oxidase SOURCE: Pig kidney REFERENCE: V. Massey, G. Palmer, C. H. P. H. Sands, Biochim. Biophys. Library ,8_ (1966). 5. Curve 1: Oxidized enzyme. Curve 2: After addition of 16 moles Dproline and kOO moles of A'-pyrroline 2-carboxylic acid. Curve 3: After 95 moles of Na 2 S 2 O^.
Atlas of Protein Spectra in the Ultraviolet and Visible Regions by Donald M. Kirschenbaum