Download e-book for iPad: Atlas of Protein Spectra in the Ultraviolet and Visible by Donald M. Kirschenbaum

By Donald M. Kirschenbaum

ISBN-10: 0306673029

ISBN-13: 9780306673023

After you have obvious the spectrum of 1 protein you may have visible the spectra of all professional­ teins. Or so it'll look. whereas the overall features of the absorption curve might sound to be comparable for all proteins (i. e. , in acid and impartial answer 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 transformations which are obvious while the spectra of many proteins are in comparison. it really is those adjustments which replicate alterations in amino acid content material and within the milieu during which the protein has been dissolved. The spectra during this booklet supply samples of those refined spectral ameliorations and allow comparisons to be made. This publication was once ready to have its index learn and its contents stated. 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 these types of 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 mentioned via species, tissues, and the organs from which they have been taken. There also are "environmental" indicies on the topic of the remedy the proteins bought ahead of having their spectra taken. Technical details referring to instrumentation is missing.

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Extra info for Atlas of Protein Spectra in the Ultraviolet and Visible Regions

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NAME: Albumin, Lysozyme, Trypsin, Pepsin, Ovalbumin SOURCE: REFERENCE: L. Berrens and E. Bleumink, Arch. , 150 (1965). Int. 0. A: B: C: D: E: Protein Lysozyme. Trypsin. Pepsin. Ovalbumin. Albumin. 05%. NAME: Albumin SOURCE: Human serum REFERENCE: W. M. Larrson, and T . H . Mead, J. Gen. Virol. , 399 (1968). 02 M phosphate buffer, pH 7 - 8 . Brain extract. 35 >ig/ml MA. 500 Mg/nil albumin. kO MgMl RNA. NAME: Albumin SOURCE: Human serum REFERENCE: W . L . Hughes, Jr. and R. Straessle, J. Am. Chem.

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. NAME: D-Amino Acid Oxidase SOURCE: Pig kidney REFERENCE: V.

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. : FAD 0,000069 M. : Mixed with excess apoenzyme. 001 M. NAME: D-Amino Acid Oxidase SOURCE: Pig kidney REFERENCE: K. Yagi and N .

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Atlas of Protein Spectra in the Ultraviolet and Visible Regions by Donald M. Kirschenbaum

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