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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 2 (1996), S. 233-242 
    ISSN: 1075-4261
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Polarized Raman scattering measurements have been made of a single crystal of AZT (3′-azido-3′-deoxythymidine) by the use of a Raman microscope with the 488.0 nm exciting beam from an argon-ion laser. The AZT crystal belongs to the space group P21 (monoclinic), and Raman scattering intensities, corresponding to the aa, bb, c′c′, and bc′ components of the crystal Raman tensor, have been determined for each prominent Raman band. Here, c′-axis was defined as an axis perpendicular to the a-axis in the ac plane. From these experimental data, and on the basis of the known crystal structure, localized Raman tensors have been determined, which are assignable to azido vibrations at 2088 and 1259 cm-1, to thymine at 1666, 1392, 1238, 771, and 495 cm-1 and deoxyribose vibrations at 870, 849 and 739 cm-1. The knowledge of these localized Raman tensors are considered to be useful for probing the orientation of the AZT molecule in a biological system involving it. © 1996 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 61-71 
    ISSN: 1075-4261
    Keywords: L-tyrosine ; polarized Raman spectra ; Raman tensor ; ab initio MO calculation ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Polarized Raman scattering measurements have been made of a single crystal of L-tyrosine by the use of a Raman microscope with the 488.0-nm exciting beam from an argon ion laser. The L-tyrosine crystal belongs to the space group P212121 (orthorhombic), and Raman scattering intensities corresponding to the aa, bb, cc, ab and ac components of the crystal Raman tensor have been determined for each prominent Raman band. A similar set of measurements has been made of L-tyrosine-d4, in which four hydrogen atoms on the benzene ring are replaced by deuterium atoms. The effects of NH3 → ND3 and OH → OD on the Raman spectrum have also been examined. In addition, depolarization ratios of some bands of L-tyrosine in aqueous solutions of pH 13 and pH 1 were examined. For comparison with these experimental results, on the other hand, ab initio molecular orbital calculations have been made of the normal modes of vibration and their associated polarizability oscillations of the L-tyrosine molecule. On the basis of these experimental data and by referring to the results of the calculations, discussions have been presented on the Raman tensors associated to some Raman bands, including those at 829 cm-1 (benzene ring breathing), 642 cm-1 (benzene ring deformation), and 432 cm-1 (Cα-Cβ-Cγ bending). © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 61-71, 1998
    Additional Material: 5 Ill.
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  • 3
    ISSN: 0263-6484
    Keywords: Cortisone ; immature intestine ; carbohydrase concentration ; de novo synthesis ; turnover ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Hydrocortisone administration to infant rats enhanced cellobiase and maltase activities and induced precocious expression of sucrase and trehalase activities along the length of the small intestine. These activity changes reflected proportional concentration increases in the enzymes lactase (EC 3.2.1.23), maltase/glucoamylase (EC 3.2.1.20) and sucrase-isomaltase (EC 3.2.1.48/10). Administration of an equivalent tracer dose of [3H]leucine (by body weight) to control and hydrocortisone-treated infant rats resulted in greater accumulation of label in the carbohydrase pools of the treated rats, suggesting their increased de novo synthesis. The increased concentrations of lactase and maltase/glucoamylase induced by exogenous hydrocortisone were matched by the presence of corresponding greater amounts of label in their brush border pools. Accumulation of label in each of the lactase, maltase/glucoamylase and sucrase-isomaltase pools was generally similar in the hydrocortisone-treated rats, suggesting equivalent stimulation of their synthesis as a group by the humoral agent. The turnover rats of the carbohydrates as a group were found to be similar and did not appear to differ in control and hydrocortisone-treated rats. Total protein synthesis rates were slightly greater in the intestine of the hydrocortisone-treated group of rats.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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