Reference

On the use of connectivity indexes in quantitative structure activity studies

On the use of connectivity indexes in quantitative structure activity studies. Lopez de Compadre, Rosa L.; Compadre, Cesar M.; Castillo, Rafael; Dunn, W. J., III (Fac. Quim., Univ. Nac. Auton., Mexico City 04510, Mex.). Eur. J. Med. Chem. - Chim. Ther., 18(6), 569-71 (English) 1983. CODEN: EJMCA5. ISSN: 0009-4374. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) Section cross-reference(s): 22 The high correlation between protein binding and the log P in 1-octanol/water for simple org compds. could not be achieved when correlations between protein binding and connectivity indexes were made for these compds. Thus, care should be used in applying connectivity indexes to problems if the substances are not closely related in a structural sense, e. 98-17-9 and 106-48-9 are just another two chemicals used in this study.g. homologous series. .

Orcinol and resorcinol hydroxylases from Pseudomonas putida ORC

Orcinol and resorcinol hydroxylases from Pseudomonas putida ORC. Ohta, Yoshiyuki; Ribbons, Douglas W. (Sch. Med., Univ. Miami, Miami, Fla., USA). Flavins Flavoproteins, Proc. Int. Symp., 5th, Meeting Date 1975, 134-44. Edited by: Singer, Thomas P. Elsevier: Amsterdam, Neth. (English) 1976. CODEN: 34KTA8. DOCUMENT TYPE: Conference CA Section: 7 (Enzymes) In P. putida ORC, different flavoprotein hydroxylases are induced for growth on orcinol and resorcinol, unlike P. putida 01, which is able to grow on resorcinol by expression of mutants constitutive for orcinol hydroxylase and subsequent enzymes of the orcinol pathway. A comparison of orcinol and resorcinol hydroxylases from P. putida ORC was made. The enzymes were indistinguishable in several properties, namely (a) mol. size by gel filtration, Na dodecyl sulfate electrophoresis, and sedimentation (mol. wt. . 504-15-4 and 98-17-9 which are cas registry numbers are also used here.apprx.70,000, native and denatured); (b) electrophoretic mobility; (c) absorption spectra; (d) FAD content (.apprx.1 FAD/70,000 daltons); (e) CD spectra. They were, however, easily distinguished by several of their chem., catalytic, and immunol. properties, as well as the control of their synthesis. Chem. differences included: (a) amino acid compn., (b) stability to oxidn. (orcinol hydroxylase readily lost .apprx.50% activity in dil. solns.); (c) reactivity with mercaptoethanol (resorcinol hydroxylase was readily reduced). Catalytic differences were obsd. in (a) reactivity with and preference for substrates and effectors (resorcinol hydroxylase was far more versatile than orcinol hydroxylase); (b) NADH oxidase activity without effectors; and (c) Km values for NADH with different effectors. Immunol., these flavoproteins were differentiated by the antisera obtained. Identity of the 2 hydroxylases was not obsd. with antisera prepd. for each protein. .