Bovine serum albumin–vanadium complex hybrid: Synthesis, crystal structure, SOD activities and asymmetric catalytic oxidation of sulfides

Polyhedron ◽  
2019 ◽  
Vol 162 ◽  
pp. 81-90 ◽  
Author(s):  
Jingnan Shi ◽  
Yi Wei ◽  
Yuzhen Zhang ◽  
Jie Tang ◽  
Hedong Bian ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Catalytic Oxidation ◽  
Bovine Serum ◽  
Vanadium Complex ◽  
Asymmetric Catalytic ◽  
Oxidation Of Sulfides ◽  
Complex Hybrid

Enantio and diastereoselectivity in the periodate oxidation of sulfides catalyzed by bovine serum albumin. 2

1986 ◽  
Vol 51 (6) ◽  
pp. 891-895 ◽  
Author(s):  
Stefano Colonna ◽  
Stefano Banfi ◽  
Rita Annunziata ◽  
Luigi Casella
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Periodate Oxidation ◽  
Oxidation Of Sulfides

scholarly journals pH DEPENDENT STRUCTURES OF BOVINE SERUM IN SOLUTION BY SMALL ANGLE NEUTRON SCATTERING

2021 ◽  
Vol 83 (2) ◽  
pp. 117-123
Author(s):  
Arum Patriati ◽  
Edy Giri Rachman Putra
Keyword(s):  
Crystal Structure ◽  
Protein Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Neutron Scattering ◽  
Small Angle ◽  
Bovine Serum ◽  
Small Angle Neutron Scattering ◽  
Static State ◽  
Ph Dependent

The pH-dependent structures of the bovine serum albumin (BSA), under physiological conditions that permit enzymatic activity, were investigated by small-angle neutron scattering (SANS). The unfolding behavior of BSA in solution is important to understand the mechanism of protein aggregation due to protein conformational change. The information of protein structure is crucial to design the perfect protein-based drug delivery device. This information will be useful as a complementary data of BSA crystal structure in static state. The structure of BSA in solution was found to be heart shaped, nearly identical to bovine serum albumin crystal structure. The globular heart shaped structure of BSA was still maintained at alkaline pH range of 7 to 11. It underwent partial unfolding at pH 5 and continued to unfold at pH 3. The unfolded-structure of BSA shows that the globular structure started to change into a cylinder-like structure at pH 3 which was clearly shown in Kratky plot. These results were confirmed with ab initio low-resolution shape calculation model analysis using GNOM and DAMMIF in obtaining the three-dimensional protein structure model.

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