@article {1716,
	title = {Stereochemical studies of adrenergic drugs. Optically active derivatives of imidazolines.},
	journal = {J Med Chem},
	volume = {19},
	year = {1976},
	month = {1976 Dec},
	pages = {1382-4},
	abstract = {<p>The synthesis of (R)-(+)-4-methyl-2-(1-naphthylmethyl)imidazoline hydrochloride (2) and (S)-(-)-4-methyl-2-(1-naphthylmethyl)imidazoline hydrochloride (3) is presented. The synthesis involves the preparation of (R)-(+)- and (S)-(-)-1,2-diaminopropane dihydrochloride and then allowing the appropriate diaminopropane to react with ethyl 1-naphthyliminoacetate hydrochloride in the presence of triethylamine. The parent compound, naphazoline, is a potent alpha-adrenoreceptor agonist (-log ED50 = 7.22), whereas the methylated derivatives, 2 and 3, were moderately potent antagonists (pA2 = 5.6 and 5.8, respectively) of the alpha-adrenoreceptor. Compounds 2 and 3 also produced blockade of the response to histamine on the rabbit aorta, but at concentrations approximately 20 times higher than necessary to produce equal blockade of the alpha-adrenoreceptor.</p>},
	keywords = {Animals, Aorta, Histamine H1 Antagonists, Imidazoles, In Vitro Techniques, Muscle, Smooth, Naphazoline, Phenylephrine, Rabbits, Receptors, Adrenergic, Receptors, Adrenergic, alpha, Stereoisomerism},
	issn = {0022-2623},
	author = {Miller, D D and Hsu, F L and Ruffolo, R R and Patil, P N}
}
@article {1738,
	title = {Bile acids. XLVII. 12alpha-Hydroxylation of precursors of allo bile acids by rabbit liver microsomes.},
	journal = {Biochim Biophys Acta},
	volume = {409},
	year = {1975},
	month = {1975 Nov 21},
	pages = {249-57},
	abstract = {<p>Rabbit liver microsomal preparations fortified with 0.1 mM NADPH effectively promote hydroxylation of [3beta-3H]- or [24-14C]allochenodeoxycholic acid or [5alpha,6alpha-3H2]5alpha-cholestane-3alpha,7alpha-diol to their respective 12alpha-hydroxyl derivatives in yields of about 25 or 65\% in 60 min. Minor amounts of other products are formed from the diol. The requirements for activity of rabbit liver microsomal 12alpha-hydroxylase resemble those of rat liver microsomes. Of a number of enzyme inhibitors studied only p-chloromercuribenzoate demonstrated a marked ability to inhibit the reaction with either tritiated substrate. There was no difference in the quantity of product produced from the tritiated acid or the 14C-labeled acid. No clear sex difference was found in activity of the enzyme, nor was an appreciable difference noted in activity of the enzyme between mature and immature animals.</p>},
	keywords = {Aging, Animals, Bile Acids and Salts, Female, Kinetics, Male, Microsomes, Liver, Mixed Function Oxygenases, NADP, Oxidation-Reduction, Rabbits, Sex Factors},
	issn = {0006-3002},
	author = {Ali, S S and Elliott, W H}
}
