Structural aspects of aqueous tetraalkylammonium salt solutions

1973 ◽  
Vol 2 (2-3) ◽  
pp. 253-276 ◽  
Author(s):  
Wen-Yang Wen
Keyword(s):  
Tetraalkylammonium Salt ◽  
Salt Solutions ◽  
Structural Aspects

scholarly journals The thermal stability of oligonucleotide duplexes is sequence independent in tetraalkylammonium salt solutions: application to identifying recombinant DNA clones

1988 ◽  
Vol 16 (10) ◽  
pp. 4637-4650 ◽  
Author(s):  
Kenneth A. Jacobs ◽  
Richard Rudersdorf ◽  
Suzanne D. Neill ◽  
Joseph P. Dougherty ◽  
Eugene L. Brown ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Recombinant Dna ◽  
Tetraalkylammonium Salt ◽  
Salt Solutions ◽  
Thermal Stability Of

Salt-specific effects observed in calorimetric studies of alkali and tetraalkylammonium salt solutions of poly(thiophen-3-ylacetic acid)

2015 ◽  
Vol 17 (4) ◽  
pp. 2475-2483 ◽  
Author(s):  
Gregor Hostnik ◽  
Vojko Vlachy ◽  
Dmitrij Bondarev ◽  
Jir̆í Vohlídal ◽  
Janez Cerar
Keyword(s):  
Tetraalkylammonium Salt ◽  
Salt Solutions ◽  
Specific Effects ◽  
Calorimetric Studies ◽  
Ylacetic Acid ◽  
Acid Salts

Differences in hydration of counterions are blamed for strong salt-specific effects produced upon dilution and mixing of poly(thiophene-3-ylacetic acid) salts with simple salts.

Structural aspects of osmoregulation in porphyra

1978 ◽  
Vol 36 (2) ◽  
pp. 412-413
Author(s):  
C. Wiencke ◽  
A. Lauchli
Keyword(s):  
Culture Medium ◽  
Point Of View ◽  
Chemical Fixation ◽  
Cellular Organization ◽  
Osmotic Adaptation ◽  
Osmotic Balance ◽  
Activity Of Enzymes ◽  
Osmotic Agents ◽  
Vacuolar System ◽  
Structural Aspects

Osmoregulatory mechanisms in algae were investigated mainly from a physiological point of view (KAUSS 1977, HELLEBUST 1976). In Porphyra two osmotic agents, i. e. floridoside/isofloridoside (KAUSS 1968) and certain ions, such as K+ and Na+(EPPLEY et al. 1960) are considered for osmotic balance. Accumulations of ions (particularly Na+) in the cytoplasm during osmotic adaptation is improbable, because the activity of enzymes is generally inhibited by high ionic concentrations (FLOWERS et al. 1977).The cellular organization of Porphyra was studied with special emphasis on the development of the vacuolar system under different hyperosmotic conditions. Porphyra was cultivated at various strengths of the culture medium ASP 12 (PROVASOLI 1961) ranging from normal to 6 times concentrated (6x) culture medium. Por electron microscopy freeze fracturing was used (specimens fixed in 2% glutaraldehyde and incubated in 30% glycerol, preparation in a BALZERS BA 360 M apparatus), because chemical fixation gave poor results.

Molecular Structure of the Outermost Cell Wall Component of Spirillum Serpens

1977 ◽  
Vol 35 ◽  
pp. 342-343
Author(s):  
Wah Chiu ◽  
David Grano
Keyword(s):  
Molecular Structure ◽  
Cell Wall ◽  
Outer Membrane ◽  
Gel Electrophoresis ◽  
Electron Microscopic Examination ◽  
Electron Microscopic ◽  
Cell Wall Component ◽  
Protein Components ◽  
Exposure Technique ◽  
Structural Aspects

The periodic structure external to the outer membrane of Spirillum serpens VHA has been isolated by similar procedures to those used by Buckmire and Murray (1). From SDS gel electrophoresis, we have found that the isolated fragments contain several protein components, and that the crystalline structure is composed of a glycoprotein component with a molecular weight of ∽ 140,000 daltons (2). Under an electron microscopic examination, we have visualized the hexagonally-packed glycoprotein subunits, as well as the bilayer profile of the outer membrane. In this paper, we will discuss some structural aspects of the crystalline glycoproteins, based on computer-reconstructed images of the external cell wall fragments.The specimens were prepared for electron microscopy in two ways: negatively stained with 1% PTA, and maintained in a frozen-hydrated state (3). The micrographs were taken with a JEM-100B electron microscope with a field emission gun. The minimum exposure technique was essential for imaging the frozen- hydrated specimens.

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