Synthesis and Properties of pH‐Dependent Gemini Surfactants Containing Multiple Carboxyl Groups

2020 ◽  
Vol 23 (2) ◽  
pp. 263-271 ◽  
Author(s):  
Longyin Qiao ◽  
Wanjing Zhang ◽  
Libo Xu ◽  
Fu Han ◽  
Yawen Zhou ◽  
...  
Author(s):  
Marco Scarzello ◽  
Marc Stuart ◽  
Jaap Klijn ◽  
Anno Wagenaar ◽  
Jan Engberts

1973 ◽  
Vol 136 (4) ◽  
pp. 919-926 ◽  
Author(s):  
Jack McLaughlin ◽  
Kenneth R. Case ◽  
H. Bruce Bosmann

Synaptic vesicles isolated from guinea-pig cerebral cortex had an electrophoretic mobility of −3.55μm·s-1·V-1·cm in saline–sorbitol, pH7.2, at 25°C (ionic strength 0.015g-ions/1). The mobility was pH-dependent, varied with ionic strength and indicated that the vesicular surface contained weak acidic functions with a pKa in the range 3.0–3.8. Although the vesicular surface was determined to be highly negatively charged, treatment with neuraminidase had no effect on mobility and indicated that the relatively strong carboxyl groups of sialic acid do not contribute significantly to vesicular electrokinetic properties. Treatment of synaptic vesicles with trypsin or trypsinized concanavalin A resulted in increases in mobility, but treatment with ribonuclease, deoxyribonuclease, chrondroitinase ABC or hyaluronidase had no significant effect on mobility. Mn2+or Ca2+was more effective in decreasing vesicle mobility than was Mg2+, Sr2+or Ba2+. The electrokinetic properties of the synaptic vesicle surface are discussed and contrasted with the properties of the synaptosomal membrane.


2007 ◽  
Vol 111 (19) ◽  
pp. 5204-5211 ◽  
Author(s):  
Jaap E. Klijn ◽  
Stuart ◽  
Marco Scarzello ◽  
Anno Wagenaar ◽  
Jan B. F. N. Engberts

2018 ◽  
Vol 83 (3) ◽  
pp. 1320-1327 ◽  
Author(s):  
Tanasak Kaewsomboon ◽  
Shuhei Nishizawa ◽  
Takashi Kanamori ◽  
Hideya Yuasa ◽  
Akihiro Ohkubo

Langmuir ◽  
2006 ◽  
Vol 22 (6) ◽  
pp. 2558-2568 ◽  
Author(s):  
Marco Scarzello ◽  
Jaap E. Klijn ◽  
Anno Wagenaar ◽  
Marc C. A. Stuart ◽  
Ron Hulst ◽  
...  

Polymers ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 511 ◽  
Author(s):  
Sayaka Fukui ◽  
Tomoyasu Hirai ◽  
Yoshinobu Nakamura ◽  
Syuji Fujii

Near-monodispersed micrometer-sized polystyrene (PS) particles carrying amidino and carboxyl groups on their surfaces were synthesized by soap-free emulsion polymerization using an amphoteric free radical initiator. The resulting amphoteric PS particles were characterized in terms of diameter, morphology, disperibility in aqueous media and surface charge using scanning electron microscopy (SEM), optical microscopy (OM), sedimentation rate and electrophoretic measurements. At pH 2.0, where the amidino groups are protonated (positively charged), and at pH 11.0, where the carboxyl groups are deprotonated (negatively charged), the PS particles were well dispersed in aqueous media via electrostatic repulsion. At pH 4.8, where the surface charges are neutral, the PS particles were weakly aggregated. Furthermore, it was confirmed that the PS particles can function as a pH-sensitive foam stabilizer: foamability and foam stability were higher at pH 2.0 and 4.8, where the PS particles can be adsorbed to the air–water interface, and lower at pH 11.0, where the PS particles tend to disperse in bulk aqueous medium. SEM and OM studies indicated that hexagonally close-packed arrays of PS particles were formed on the bubble surfaces and moiré patterns were observed on the dried foams. Moreover, the fragments of dried foams showed iridescent character under white light.


1964 ◽  
Vol 30 (1) ◽  
pp. 131-145 ◽  
Author(s):  
M. GINSBURG ◽  
M. IRELAND

SUMMARY Association of oxytocin and arginine vasopressin with protein in bovine and rabbit neurohypophysial extracts has been studied by co-precipitation of the hormones with protein on addition of NaCl, by gel filtration and by dialysis. Although precipitates formed by addition of NaCl (2·5–20 g./100 ml.) to bovine neurohypophysial extracts at pH 3·1 contain both hormones, oxytocin and arginine vasopressin were partially separated at 5·0 g. NaCl/100 ml. when the proportion of oxytocin precipitated was approximately double that of arginine vasopressin. No precipitate formed on addition of NaCl (15 g./100 ml.) to bovine neurohypophysial extract at pH 5.8. Experiments by gel filtration and dialysis showed that the binding of oxytocin and vasopressin to protein in neurohypophysial extracts is pH dependent and is maximal in the range pH 5·2–5·8. Dilution of a solution containing neurohypophysial hormones and protein results in dissociation of the complexes and this could account for differences observed in experiments with bovine and rabbit neurohypophysial extracts. It is suggested that the mode of binding between the hormones and protein is ionic association between the cationic free terminal NH2 of the cystine residue in the hormones and free carboxyl groups in protein.


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