Role of Surfactant Micelle Charge in Protein Denaturation and Surfactant-Induced Skin Irritation

Author(s):  
P Somasundaran ◽  
C Vincent ◽  
L Yang ◽  
X Hua ◽  
K Ananthapadmanabhan ◽  
...  
2021 ◽  
Vol 7 ◽  
Author(s):  
Muhammad Nadeem Yousaf ◽  
Hamid Ehsan ◽  
Ahmad Muneeb ◽  
Ahsan Wahab ◽  
Muhammad K. Sana ◽  
...  

Pancreatic cancer is one of the most aggressive malignancies of the digestive tract and carries a poor prognosis. The majority of patients have advanced disease at the time of diagnosis. Surgical resection offers the only curative treatment, but only a small proportion of patients can undergo surgical resection. Radiofrequency ablation (RFA) is a well-known modality in the management of solid organ tumors, however, its utility in the management of pancreatic cancer is under investigation. Since the past decade, there is increasing use of RFA as it provides a feasible palliation treatment in the management of unresectable pancreatic cancer. RFA causes tumor cytoreduction through multiple mechanisms such as coagulative necrosis, protein denaturation, and activation of anticancer immunity. The safety profile of RFA is controversial because of the high risk for complications, however, small prospective and retrospective studies have shown promising results in its applicability for palliative management of unresectable pancreatic malignancies. In this review, we discuss different approaches of RFA, their indications, technical accessibility, safety, and major complications in the management of unresectable pancreatic cancer.


2001 ◽  
Vol 68 (3) ◽  
pp. 471-481 ◽  
Author(s):  
CATHERINE SCHORSCH ◽  
DEBORAH K. WILKINS ◽  
MALCOLM G. JONES ◽  
IAN T. NORTON

The aim of the present work was to investigate the role of whey protein denaturation on the acid induced gelation of casein. This was studied by determining the effect of whey protein denaturation both in the presence and absence of casein micelles. The study showed that milk gelation kinetics and gel properties are greatly influenced by the heat treatment sequence. When the whey proteins are denatured separately and subsequently added to casein micelles, acid-induced gelation occurs more rapidly and leads to gels with a more particulated microstructure than gels made from co-heated systems. The gels resulting from heat-treatment of a mixture of pre-denatured whey protein with casein micelles are heterogeneous in nature due to particulates formed from casein micelles which are complexed with denatured whey proteins and also from separate whey protein aggregates. Whey proteins thus offer an opportunity not only to control casein gelation but also to control the level of syneresis, which can occur.


1994 ◽  
Vol 50 (3) ◽  
pp. 267-275 ◽  
Author(s):  
Carmen G. Sotelo ◽  
Santiago P. Aubourg ◽  
Ricardo I. Perez-Martin ◽  
Jose Manuel Gallardo

2012 ◽  
Vol 67 (1) ◽  
pp. 28-35 ◽  
Author(s):  
Mariette J. C. Nagtegaal ◽  
Stefanie E. Pentinga ◽  
Joop Kuik ◽  
Sanja Kezic ◽  
Thomas Rustemeyer
Keyword(s):  

2008 ◽  
Vol 8 (1) ◽  
pp. 29 ◽  
Author(s):  
Catherine Michaux ◽  
Jenny Pouyez ◽  
Johan Wouters ◽  
Gilbert G Privé

1962 ◽  
Vol 45 (4) ◽  
pp. 777-799 ◽  
Author(s):  
Roger Milkman

Day old Drosophila pupae were subjected to a variety of closely controlled temperature shocks. Twenty-five hours after puparium formation (at 23°), temperatures from 39.5–41.5° (Q1 = 2.3) differentially disturb the formation of the posterior crossvein. Three other separate treatments disturb posterior crossvein formation: treatments in the range 36.0–37.0° at 25 hours; 37.3–37.8° at 25 hours; and 39.5–41.5° at 19 hours. Certain qualitative effects are associated with certain temperatures: elliptical holes are seen in wings of flies exposed 25 hours after puparium formation to temperatures from 37.3–37.8°. Anterior crossvein defects ensue if animals are similarly exposed to temperatures from 37.9–38.2°. Within the physiological range, animals raised at higher temperatures are more resistant to the effects of temperatures at 39.5–41.5°. An extremely rapid temperature adaptation by exposures to temperatures in the range 31–38° results in markedly greater resistance to heat shock; here resistance to production of crossvein defects increases faster than to death. The association between qualitative effects and treatment temperatures is modified by changing the temperature at which the animals spend their first day of pupal life. Summation experiments support conclusions drawn from the simpler experiments. Genetic variation and interspecific variation are discussed in the present context, as well as implications of the role of protein denaturation in the biological effects of high temperatures and further, more general experiments.


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