Two Dimensional Auto-Organized Nanostructure Formation of Hyaluronate on Bovine Serum Albumin Monolayer and Its Surface Tension

Langmuir ◽  
2000 ◽  
Vol 16 (9) ◽  
pp. 4272-4278 ◽  
Author(s):  
Tsuyoshi Nonogaki ◽  
Shouhong Xu ◽  
Shin-ichi Kugimiya ◽  
Shizuko Sato ◽  
Isamu Miyata ◽  
...  
2003 ◽  
Vol 29 (10-11) ◽  
pp. 711-716 ◽  
Author(s):  
Shouhong Xu ◽  
Shizuko Sato ◽  
Isamu Miyata ◽  
Junpei Yamanaka ◽  
Masakatsu Yonese

RSC Advances ◽  
2017 ◽  
Vol 7 (42) ◽  
pp. 26250-26255 ◽  
Author(s):  
Arun Singh Patel ◽  
Praveen Mishra ◽  
Pawan K. Kanaujia ◽  
Syed Shariq Husain ◽  
G. Vijaya Prakash ◽  
...  

The resonance energy transfer (RET) from tryptophan present in bovine serum albumin (BSA) to two dimensional (2D) nanomaterials has been reported.


RSC Advances ◽  
2016 ◽  
Vol 6 (24) ◽  
pp. 19700-19706 ◽  
Author(s):  
Gongke Wang ◽  
Huimin Hou ◽  
Ye Chen ◽  
Changling Yan ◽  
Guangyue Bai ◽  
...  

The interactions between decyl-β-d-glucopyranoside (DG) and bovine serum albumin (BSA), in aqueous media, were investigated through the use of surface tension, steady-state fluorescence, and UV-vis absorption spectroscopy measurements.


2021 ◽  
pp. 118305
Author(s):  
Thu Thi-Yen Le ◽  
Siam Hussain ◽  
Ruey-Yug Tsay ◽  
Boris A. Noskov ◽  
Alexander Akentiev ◽  
...  

2001 ◽  
Vol 68 (3) ◽  
pp. 483-497 ◽  
Author(s):  
PALATASA HAVEA ◽  
HARJINDER SINGH ◽  
LAWRENCE K. CREAMER

Bovine β-lactoglobulin (β-lg), α-lactalbumin (α-la) and bovine serum albumin (BSA), dispersed in ultrafiltration permeate, that had been prepared from whey protein concentrate solution (100 g/kg, pH 6·8), were heated at 75 °C. The consequent protein aggregation was studied by one-dimensional (1D) and two-dimensional (2D) polyacrylamide gel electrophoresis (PAGE). When 100 g β-lg/kg permeate solution was heated at 75 °C, cooled and examined, large aggregates were observed. These aggregates were partially dissociated in SDS solution to give monomers, disulphide-bonded dimers, trimers and larger aggregates. When mixtures of β-lg and α-la or BSA were heated, homopolymers of each protein as well as heteropolymers of these proteins were observed. These polymer species were also observed in a heated mixture of the three proteins. Two-dimensional PAGE of mixtures demonstrated that these polymers species contained disulphide-bonded dimers of β-lg, α-la and BSA, and 1:1 disulphide-bonded adducts of α-la and β-lg, or BSA. These results are consistent with a mechanism in which the free thiols of heat-treated β-lg or BSA catalyse the formation of a range of monomers, dimers and higher polymers of α-la. It is likely that when whey protein concentrate is heated under the present conditions, BSA forms disulphide-bonded strands ahead of β-lg and that α-la aggregation with β-lg and with itself is catalysed by the heat-induced unfolded BSA and β-lg.


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