Reactivity of silanol group on siloxane oligomers for designing molecular structure and surface wettability

2021 ◽  
Vol 97 (3) ◽  
pp. 734-742
Author(s):  
Daisuke Kino ◽  
Kenji Okada ◽  
Yasuaki Tokudome ◽  
Masahide Takahashi ◽  
Luca Malfatti ◽  
...  
Author(s):  
Wah Chiu ◽  
David Grano

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.


1963 ◽  
Vol 60 ◽  
pp. 52-55
Author(s):  
István Kiss ◽  
Lajos Matus ◽  
István Opauszky

Planta Medica ◽  
2014 ◽  
Vol 80 (10) ◽  
Author(s):  
S Groscurth ◽  
T Kühn ◽  
P Kessler ◽  
V Rukachaisirikul

1966 ◽  
Vol 16 (01/02) ◽  
pp. 018-031 ◽  
Author(s):  
S Sherry ◽  
Norma Alkjaersig ◽  
A. P Fletcher

SummaryComparative studies have been made of the esterase activity of plasmin and the streptokinase-activator of plasminogen on a variety of substituted arginine and lysine esters. Human plasmin preparations derived by different methods of activation (spontaneous in glycerol, trypsin, streptokinase (SK) and urokinase) are similar in their esterase activity; this suggests that the molecular structure required for such esterase activity is similar for all of these human plasmins. Bovine plasmin, on the other hand, differs from human plasmin in its activity on several of the substrates studied (e.g., the methyl esters of benzoyl arginine and tosyl, acetyl and carbobenzoxy lysine), a finding which supports the view that molecular differences exist between the two animal plasmins. The streptokinase-activator hydrolyzes both arginine and lysine esters but the ratios of hydrolytic activity are distinct from those of plasmin and of other activators of plasminogen. The use of benzoyl arginine methyl ester as a substrate for the measurement of the esterase activity of the streptokinase-activator is described.


Author(s):  
Saraa Muwafaq Ibrahim ◽  
Ziad T. Abd Ali

Batch experiments have been studied to remove methylene blue dye (MB) from aqueous solution using modified bentonite. The modified bentonite was synthesized by replacing exchangeable calcium cations in natural bentonite with cationic surfactant cetyl trimethyl ammonium bromide (CTAB). The characteristics of modified bentonite were studied using different analysis such as Scanning electronic microscopy (SEM), Fourier transform infrared spectrometry (FTIR) and surface area. Where SEM shows the natural bentonite has a porous structure, a rough and uneven appearance with scattered and different block structure sizes, while the modified bentonite surface morphology was smooth and supplemented by a limited number of holes. On other hand, (FTIR) analysis that proved NH group aliphatic and aromatic group of MB and silanol group are responsible for the sorption of contaminate. The organic matter peaks at 2848 and 2930 cm-1 in the spectra of modified bentonite which are sharper than those of the natural bentonite were assigned to the CH2 scissor vibration band and the symmetrical CH3 stretching absorption band, respectively, also the 2930 cm-1 peak is assigned to CH stretching band. The batch study was provided the maximum removal efficiency (99.99 % MB) with a sorption capacity of 129.87 mg/g at specified conditions (100 mg/L, 25℃, pH 11 and 250rpm). The sorption isotherm data fitted well with the Freundlich isotherm model. The kinetic studies were revealed that the sorption follows a pseudo-second-order kinetic model which indicates chemisorption between sorbent and sorbate molecules.


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