Forty-First Annual Meeting March 2-6, 1997 Ernest N. Morial Convention Center New Orleans, Louisiana. Tuesday Symposia and Posters, Part IV
Identifieur interne : 002099 ( Main/Corpus ); précédent : 002098; suivant : 002100Forty-First Annual Meeting March 2-6, 1997 Ernest N. Morial Convention Center New Orleans, Louisiana. Tuesday Symposia and Posters, Part IV
Auteurs :Source :
- Biophysical Journal [ 0006-3495 ] ; 1997.
Url:
DOI: 10.1016/S0006-3495(97)78739-3
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Behrens. H. Otto, R. Mollaaghababa*, U. Alexiev, H.G. Khorana* and M.P. CELLS. ((Timothy Ragan', Peter T.C. So I and Enrico Gratton l W. Green St.</editor><imprint><biblScope unit="volume">77</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page">61801</biblScope><date type="published" when="1110"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">E</forename><forename type="middle">H K</forename><surname>Stelzer</surname></persName></author><author><persName><forename type="first">S</forename><surname>Lindek</surname></persName></author></analytic><monogr><title level="j">Opt. Commun</title><imprint><biblScope unit="volume">111</biblScope><biblScope unit="page" from="536" to="547"></biblScope><date type="published" when="1994"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">S</forename><surname>Lindek</surname></persName></author></analytic><monogr><title level="j">Rev. Sci. Instr</title><imprint><biblScope unit="volume">65</biblScope><biblScope unit="page" from="3367" to="3372"></biblScope><date type="published" when="1994"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">E</forename><forename type="middle">H K</forename><surname>Stelzer</surname></persName></author></analytic><monogr><title level="j">J. Microsc</title><imprint><biblScope unit="volume">179</biblScope><biblScope unit="page" from="1" to="10"></biblScope><date type="published" when="1995"></date></imprint></monogr></biblStruct><biblStruct><analytic><title level="a" type="main">Schneggenburger) We have monitored single chromaffin granules (vesicles) in bovine adrenal chromaffin cells using a non-invasive optical sectioning technique, total internal reflection microscopy (TIRFM) Using TIR, fluorescence excitation is limited to an optical slice near a glass/water interface In cells located at the interface, granules loaded with fluorescent dye such as Lysotracker Green (Molec. Probes) can be visualized near to or docked at the plasma membrane This approach has been reported to detect fusion of vesicles (Steyer & Almers, 1 2x103 M-This observation indicates that ionic and/or hydrogen bond interactions are relatively predominant in the mononmer-diner association at cH-7 5 At pH6.0, 4(C. physiological salt and no heavy metal ions, the protein exhibits monomer-dimer equilibrium, with K.(,_,)= 1106 M-; At 22°C. K,(1,2) increases only slightly to 8.6x1O M'. In the presence of 150sM Zn2'. the monomer-dimer interactions increases 100-fold at pH7.4, 22°C and physiological salt with K, I,e> The weight-average sedimentation cocfficient of SmtB increases 11% from 2.OS to 2.22S in the presence of I 50.LkM Zn2' at 22C. physiological salt and pH7 4 The functional relevance of the sclf-associated formns of SrnIt3 with. regard to DNA-binding and repressor activity in vivo are currently under investigationr Sirgle crystals of SmtB have beent grown and preliminary diffraction data obtained in an effort to solve Ats _tristure Since human apolipoprotein A-L a protein involved i lipid transfer between lipoproteis, has not boenyet cyaized, in the present study we describe how dyamic Lght scattering expeiments were usefil to determme the precsystaizadon conditions under which a crysalnucleus can be obtained. The hydrodynmic radius, diffusion coefficient, estimated molecular weight and polidispersity at different pH values were evaluated based on DLS. A quick protein aggregation is observed when the pH is closer to the isoelectric point of apoA-I, in agreement with the protein solubiity theory. For apoAl at 2 mg/ml and pH= 8.0, the calculated geometical factor H value is 4.80 x109 mol g2 cm2 moleculel. The turbidWity of apoA-I solution changes following an asymptothic line when Li2SO4 is the precipitant agent. When Li2SO4 reaches 0.37 M, apoA-I starts to aggregate and the hydrodynsmic radius increases from 12 x104 cm to 145 x104 cm Our next goal will be focused to growth these nucleus unfil they reach a suitable size for X-ray diffraction analis</title><author><persName><surname>Tu-Pos448 Total Internal Relection Fluorescence Microscopy</surname></persName></author><author><persName><surname>Tirfm</surname></persName></author><author><persName><surname>Visualizes Dynamics Of Secretory Vesicles Between</surname></persName></author><author><persName><surname>Distincr Pools In Bovine Adrenal Chromaffin Cells</surname></persName></author><author><persName><forename type="first">Robert</forename><forename type="middle">H</forename><surname>Martin</surname></persName></author><author><persName><forename type="first">Walter</forename><surname>Chow</surname></persName></author><author><persName><forename type="first">* ) ) *</forename><surname>Stuhmer</surname></persName></author><author><persName><forename type="first">Expv</forename><forename type="middle">M</forename><surname>Mpi</surname></persName></author><author><persName><forename type="first">*</forename><forename type="middle">J</forename><surname>Bolsfios-Garcia</surname></persName></author><author><persName><forename type="first">M</forename><surname>Mas-Oia</surname></persName></author><author><persName><forename type="first">A</forename><surname>Soriano-Garcla</surname></persName></author><author><persName><surname>Moreno</surname></persName></author></analytic><monogr><title level="m">Kumosinski2, and H.M. Farrell2, Jr.)). iPrairie View A&M University</title><editor>Dept. Physiol., EH8 9AG, Scotland, U.K. (Spon. R. M6xco, D.F. MEXICO. (Spons. by A. Ortega</editor><meeting><address>Tu-Pos4S2 DYNAMIC L1GHT SCAlTERING AND PRECRYSTALLIZATION OF HUMAN APOPROTEIN{A-I ; Mora-Gutierrez ; CARC, Prairie View, TX 77446 and 2USDA, ARS, ERRC, Philadelphia ; PA</address></meeting><imprint><date type="published" when="19118"></date></imprint></monogr><note>3x0. l-K sAhiie K,u.4 decreases .o 1.5x102 M. Under. these conditions, crystalie nucleus are formed when apoAl concentration is betwen 2 and 4 mg/ml and Li2SO4 kept between 0.5-1.0 M</note></biblStruct></listBibl></back></text></istex:refBibTEI></enrichments><author></author><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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