Structure and Analysis: Structure M. Klaus, Structural Characteristics of Natural and Synthetic Retinoids. M.I. Dawson and P.D. Hobbs, Synthetic Retinoic Acid Analogs: Handling and Characterization. B.P. Sani and D.L. Hill, Structural Characteristics of Synthetic Retinoids. A.P. De Leenheer and H.J. Nelis, High-Performance Liquid Chromatography of Retinoids in Blood. C.D.B. Bridges, High-Performance Liquid Chromatography of Retinoid Isomers. A.C. Ross, Separation of Fatty Acid Esters of Retinol by High-Performance Liquid Chromatography. H.C. Furr, Analysis of Retinyl Esters (Vitamin A Esters) by Reversed- Phase High-Pressure Liquid Chromatography. A.J. Clifford, A.D. Jones, and H.C. Furr, Stable Isotope Dilution Mass Spectrometry to Assess Vitamin A Status. A.P. De Leenheer and W.E. Lambert, Mass Spectrometry: Methyl Ester of Retinoic Acid (Methyl**Retinoate). G.S. Shaw and R.F. Childs, Characterization of Retinylidend Iminium Salts by High-Field 1H and 13C NMR Spectroscopy. F. Seibert, Application of Resonance Raman and Infared Difference Spectroscopy to the Study of Retinal Proteins. A.B. Barua, Analysis of Water-Soluble Compounds: Glucuronides. R. Wyss, Determination of Retinoids in Plasma by High-Performance Liquid Chromatography and Automated Column Switching. L.A. Kaplan, J.A. Miller, E.A. Stein, M.J. Stampfer, Simultaneous, High-Performance Liquid Chromatographic Analysis for Analysis of Retinol, Tocopherols, Tycophene, and ga- and ~gb-Carotene in Serum and Plasma. H. Bun, N.R. Al-Mallah, C Aubert, and J.P. Cano, High-Performance Liquid ChromatographyDetermination of Aromatic Retinoids and Isotretinoin in Biological Fluids. W.A. MacCrehan, Determination of Retinol, ~ga-Tocopherol, and ~gb-Carotene in Serum by Liquid Chromatography. H.K. Biesalski, Separation of Retinyl Esters and Their Geometric Isomers by Isocratic Adsorption High-Pressure Liquid Chromatography. Receptors, Transport, and Binding Proteins: Extracellular: S.-L. Fong and C.D.B. Bridges, Purification, Characterization, Molecular Cloning, and Sequence of Interstitial Retinol-Binding Protein. A.J. Adler, G.J. Chader, and B. Wiggert, Purification and Assay of Interphotoreceptor Retinoid-Binding Protein from Eye. Intracellular: V. Giguaaere and R.M. Evans, Identification of Receptors for Retinoids as Members of Steroid and Thyroid Hormone Receptor Family. N. Takahashi and T.R. Breitman, Retinoic Acid Acylation (Retinolyation). A.K. Daly, C.P.F. Redfern, and B. Martin, The Identification and Analysis of Retinoic Acid-Binding Proteins and Receptors from Nuclei of Mammalian Cells. A.M. Jetten, J.F. Grippo, and C. Nervi, Isolation and Binding Characteristics of Nuclear Retinoic Acid Receptors. M. Pfahl, M. Tzukerman, X.-K. Zhang, J.M. Lehmann, T. Hermann, K.N. Wills, and G. Graupner. Specific Methods: W.S. Blaner, Radioimmunoassays for Retinol-Binding Protein, Cellular Retinol-Binding Protein, and Cellular Retinoic Acid-Binding Protein. M. Newcomer and T.A. Jones, X-Ray Crytallographic Studies on Retinol-Binding Proteins. D.R. Soprano and D.S. Goodman, In Situ Hybridization of Retinoid-Binding Protein Messenger RNA. G. Siegenthaler, Gel Electrophoresis Technique for CRABP, CRBP, and RBP Analysis. C.P.F. Redfern and A.K. Daly, Purification and Analysis of Cellular Retinoic Acid-Binding Protein from Neonatal Rat Skin. C. Busch, P. Sakena, K. Funa, H. Nordlinder, and U. Eriksson, Tissue Distribution of CRBP and CRABP: Use of Monospecific Antibodies for Immunohistochemistry and cRNA for the in situ Localization of mRNA's. A.-s. Lin, S.-L. Fong, and C.D.B. Bridges, Determination of Retinoids Bound to Interstitial Retinol-Binding Protein during Visual Cycle. M. Kato, M. Okuno, and Y. Muto, Purification of Cellular Retinoic Acid-Binding Protein from Human Placenta. P. Abarzua and M.I Sherman, Evaluation of Differentiation of Embryonal Carcinoma Cells in Response to Retinoids. B.P. Sani, Parasite Retinoid-Binding Proteins. J.S. Bailey and C.-H. Siu, Purification of Cellular Retinoic Acid-Binding Proteins Types I and II from Neonatal Rat Pups. V. Matarese, M.K. Buelt, L.L. Chinander, and D.A. Bernlohr, Purification of Adipocyte Lipid-Binding Protein from Human and Murine Cells. M.A. Livrea and L. Tesoriere, Binding of 11-cis Retinaldehyde to CRALBP from Pigment Epithelium. Membrane Interactions: W. Stillwell and S.R. Wassall, Interactions of Retinoids with Phospholipid membranes: Optical Spectroscopy. S.R. Wassall and W. Stillwell, Interactions of Retinoids with Phospholipid Membranes: Electron Spin Resonance. G. Fex and G. Johannesson, Transfer of Retinol from Retinol-Binding Protein Complex to Liposomes and Across Liposomal Membrane. W.J. deGrip and F.J.M. Daemen, Exchange of Retinoids between Lipid Vesicles and Rod Outer Segment Membranes. R.R. Rando and F.W. Bangerter, Intermembraneous Transfer of Retinoids. L.M. Canfield, T.A. Fritz, and T.E. Tarara, Incorporation of ~gb-Carotene into Mixed Micelles. Enzymology and Metabolism: J.A. Olson and M.R. Lakshman, Carotenoid Conversions. L.E. Gerber and K.L. Simpson, Carotenoid Cleavage: Alternative Pathways. X. Pares and P. Julia, Isoenzymes of Alcohol Dehydrogenase in Retinoid Metabolism. A.C. Ross, Measurement of Acyl-Coenzyme A-Dependent Esterification of Retinol. M.D. Ball, Acyl-Coenzyme A-Dependent Retinol Esterification. E.H. Harrison and J.L. Napoli, Bile Salt-Independent Retinyl Ester Hydrolase Activities Associated with Membranes of Rat Tissues. W.S. Blaner and D.S. Goodman, Purification and Properties of Plasma Retinol-Binding Protein. J.L. Napoli, Quantification and Characteristics of Retinoid Synthesis from Retinol and ~gb-Carotene in TissueFractions and Established Cell Lines. M.A. Leo and C.S. Lieber, Retinol 4-Hydroxylase. D.A. Cooper, Assay of Liver Retinyl Ester Hydrolase. P.S. Bernstein and R.R. Rando, Assay of Retinoid Isomerase System of Eye. M.A. Livrea and L. Tesoriere, Assay of all-trans 11-cis Retinol Isomerase Activity in Bovine Retinal Pigment Epithelium. M.S. Levin, E. Li and J.I. Gordon, Facilitating Structure Function Analyses of Mammalian Cell Retinol-Binding Proteins by Expression in E. coli. M.A. Leo and C.S. Lieber, NAD+-Dependent Retinol Dehydrogenase in Liver Microsomes. M.L. Gubler and M.I. Sherman, Metabolism of Retinoic Acid and Retinol by Intact Cells and by Cell Extracts. G. Siegenthaler, Retinoic Acid Formation from Retinol and Retinal Metabolism in Epidermal Cells
The methods in Volumes 189 and 190 apply to the use of retinoids in basic research in molecular, cellular, and development biology and in clinical medicine.
Biochemists, nutritionists, molecular biologists, cell biologists, pharmacologists, toxicologists, oncologists, and immunologists.
- No. of pages:
- © Academic Press 1990
- 28th November 1990
- Academic Press
- eBook ISBN:
@from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
Helmut Sies, MD, PhD (hon), studied medicine at the universities of Tübingen, Munich, and Paris. He was the professor and chair of the Institute for Biochemistry and Molecular Biology I at Heinrich-Heine-University Düsseldorf, Germany, where he is now professor emeritus. He is a member of the German National Academy of Sciences Leopoldina and was the president of the North Rhine-Westphalian Academy of Sciences and Arts. He was named ‘Redox Pioneer’; was the president of the Society for Free Radical Research International (SFRRI). Helmut Sies introduced the concept of “Oxidative Stress” in 1985, and was the first to reveal hydrogen peroxide as a normal constituent of aerobic cell metabolism. His research interests comprise redox biology, oxidants, antioxidants, micronutrients.
Heinrich-Heine-University Düsseldorf, Germany
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