By Donald M. Kirschenbaum
After you have noticeable the spectrum of 1 protein you might have noticeable the spectra of all professional teins. Or so it's going to appear. whereas the overall features of the absorption curve might seem 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 answer the utmost and minimal shift to longer wavelengths), there are refined changes which are obvious while the spectra of many proteins are in comparison. it truly is those alterations which replicate adjustments in amino acid content material and within the milieu within which the protein has been dissolved. The spectra during this publication supply samples of those refined spectral adjustments and allow comparisons to be made. This booklet was once ready to have its index learn and its contents talked about. For the reader who wants to understand what a protein spectrum feels like in acid and alkaline media, after X-ray or UV irradiation, or after photo-oxidation or B-bromosuccinimide therapy, spectral representations of a lot of these experimental events etc can be found. The indicies have been ready to supply the utmost details with the minimal attempt. as well as an alphabetical directory, all spectra are observed by way of species, tissues, and the organs from which they have been taken. There also are "environmental" indicies relating to the remedy the proteins bought ahead of having their spectra taken. Technical details relating instrumentation is missing.
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Extra info for Atlas of Protein Spectra in the Ultraviolet and Visible Regions
FAD. FAD. NAME: D-Amino Acid Oxidase SOURCE: pig kidney REFERENCE: K, Yagi, Biochim. Acta Library, 8_, 210 (1966). 2. I II III IV V VI VII VIII Holoenzyme. 03 M D-alanine. 00188 M D-alanine. 00165 M D-alanine. 00132 M D-alanine. 00099 M D-alanine. 00066 M D-alanine. 00033 M D-alanine. 85 x 10"^M. NAME: D-Amino Acid Oxidase Intermediates SOURCE: Pig kidney REFERENCE: K. Yagi, Biochim. Biophys, Acta. Library, 8_, 210 (1966). 03 M D-alanine. Curve I : Type 550. Curve II : After 2 hours at 50C. Curve III : After 12 hours at 5°C.
Curve IV : Holoenzyme solution. 2 x 10"^ M. NAME: D-Amino Acid Oxidase SOURCE: PiS kidney REFERENCE: K. Yagi, M. Naoi, M. Nishikimi, and A. Kotaki, J. , Tokyo, 68, 293 (1970). 3 PH Curve I Curve II Curve III NAME: D-Amino Acid Oxidase SOURCE: Pig kidney REFERENCE: K. Yagi and U. Ohishi, J. , Tokyo, 67, 599 (1970). 05 M ammonium sulfate. Curve I Purple complex. Curve II After illumination with 553 mu light. Curve III With kkO mu light. Curve IV With 1*02 mu light. Curve V With 36k mu light. Curve VI With 287 mu light.
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^. Curve k: 18 hours after the addition of a further 500 moles of Na 2 S 2 O* per mole enzyme bound flavin.