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Synthetic application of iron acyl complexesWills, M. January 1988 (has links)
No description available.
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New chemistry of sulphonyl substituted small ringsHewkin, Cheryl T. January 1990 (has links)
No description available.
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Quorum sensing in Yersinia pseudotuberculosisBuckley, Catherine M. F. January 2002 (has links)
No description available.
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Stereoselective synthesis via iron acyl complexesEaston, R. J. C. January 1987 (has links)
No description available.
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Behavior of mixed o-acyl-n-acyl derivatives in which the reacting groups are not on adjacent carbon atomsClark, E. P. January 1926 (has links)
Thesis (Ph. D.)--University of Iowa, 1924. / Biography.
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The effect of the acidity of acyl upon the migration from nitrogen to oxygen in ortho-aminophenolsLankelma, Herman Peter, January 1925 (has links)
Thesis (Ph. D.)--University of Iowa, 1923. / Biography.
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Acyl-CoA dehydrogenases characterization of the new member isobutyryl-CoA dehydrogenase, genetic defects and correlation to thermal unfolding /Ibrahim, Nasser El-Din. January 2003 (has links) (PDF)
Konstanz, University, Diss., 2003.
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The cardiovascular effects of long chain acyl carnitines and novel ester derivativesCriddle, David N. January 1990 (has links)
No description available.
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Acyl Carrier Protein Interacts With MelittinErnst-Fonberg, Mary L., Williams, Sande G., Worsham, Lesa M.S. 18 September 1990 (has links)
Acyl carrier protein (ACP) from Escherichia coli has been shown to form complexes with melittin, a cationic peptide from bee venom. ACP is a small (Mr 8847), acidic, Ca2+-binding protein, which possesses some characteristics resembling those of regulatory Ca2+-binding proteins including interaction with melittin. Complexing between melittin and ACP which occurred both in the presence and absence of Ca2+ was evident by chemical cross-linking the two peptides, fluorescence changes (including anisotropy measurements), and inhibition by melittin of the activity of a nonaggregated fatty acid synthetase from Euglena. Also, anti-Apis mellifera antibodies which contained antibodies against melittin specifically inhibited the same enzyme system activity relative to non-immune IgG.
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Studies in the acyl enzyme of chymotrypsin : affects of substituent, pH, and temperature /Moffit, Michael Joseph January 1979 (has links)
No description available.
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