Role of trehalose in moisture-induced aggregation of bovine serum albumin

2008 ◽  
Vol 69 (3) ◽  
pp. 824-834 ◽  
Author(s):  
N JAIN ◽  
I ROY
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Induced Aggregation

scholarly journals Enhancement of Teliospore Germination in Wheat- and Wild Grass-Infecting Species of Tilletia on Activated Charcoal Medium

1998 ◽  
Vol 88 (3) ◽  
pp. 260-264 ◽  
Author(s):  
María L. Boyd ◽  
Lori M. Carris
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Activated Charcoal ◽  
Bovine Serum ◽  
Germination Percentage ◽  
Polyvinyl Pyrrolidone ◽  
Wild Grass ◽  
Teliospore Germination ◽  
Lag Period

The effect of activated charcoal as an amendment to water agar medium on teliospore germination was analyzed for two species of wheat-infecting bunts, Tilletia controversa and T. tritici, and two related wild-grass infecting species, T. bromi and T. fusca. Final percentages of teliospore germination, area under the germination progress curves (AUGPC), and a standardized AUGPC (SAUGPC) on carbon agar and water agar were compared among strains. Carbon agar (CA) significantly increased the final germination percentage of teliospores, AUGPC, and SAUGPC when compared with water agar (WA) for all taxa under study. Additionally, CA reduced significantly the incubation (i.e., lag) period when compared with WA for teliospores of T. bromi, T. controversa, and T. fusca. Bovine serum albumin and polyvinyl pyrrolidone were used as alternative chemical adsorbent amendments to WA to establish the role of activated charcoal in the medium. Only media amended with bovine serum albumin and activated charcoal improved the final germination percentage of all taxa. Polyvinyl pyrrolidone was not significantly better than water agar.

Role of bovine serum albumin in the degradation of zirconia and its allotropes coated 316L SS for potential bioimplants

2021 ◽  
Vol 258 ◽  
pp. 123859
Author(s):  
Gobi Saravanan Kaliaraj ◽  
Bavanilatha Muthaiah ◽  
Karthik Alagarsamy ◽  
Vinita Vishwakarma ◽  
A.M. Kamalan Kirubaharan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

Role of Bovine Serum Albumin-Glutaraldehyde Glue in the Formation of Anastomatic Pseudoaneurysms

2010 ◽  
Vol 26 (1) ◽  
pp. 76-81 ◽  
Author(s):  
Joshua Weiner ◽  
Shannon Widman ◽  
Zygmunt Golek ◽  
Maryann Tranquilli ◽  
John A. Elefteriades
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

scholarly journals Spectroscopic Studies on the Interaction of a Water-Soluble Cationic Porphyrin with Bovine Serum Albumin

2013 ◽  
Vol 36 (1-2) ◽  
pp. 21-26 ◽  
Author(s):  
Hamid Dezhampanah ◽  
Abdol-Khalegh Bordbar ◽  
Yadolahe Khodadusdt
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molecular Conformation ◽  
Fluorescence Emission ◽  
Water Soluble ◽  
Aggregate Formation ◽  
Cationic Porphyrin ◽  
Porphyrin Complex ◽  
Induced Aggregation

The interaction of a water-soluble cationic porphyrin, Cobalt(III) 5, 10, 15, 20-tetrakis (1-methylpyridinium-4-yl) porphyrin [Co(III)TMPyP], with bovine serum albumin (BSA) has been studied in 1 mM phosphate buffer pH 7.0 containing 5 mM NaCl by UV-vis absorption, resonance light scattering (RLS) and fluorescence spectroscopies at 25°C. The results of RLS studies represent no aggregate formation of porphyrin in the surface of BSA and low tendency of this porphyrin for aggregate formation.The binding of porphyrin complex to BSA quenches fluorescence emission of BSA via a dynamic mechanism and the quenching process obeys a linear Stern-Volmer relationship. The values of Stern-Volmer constants, KSV, was determined nearly 105M−1, that depend on BSA concentration. The average aggregation number of BSA calculated from the analysis of fluorescence quenching data indicates that absence of any porphyrin induced aggregation of BSA due to its interaction with porphyrin complex. The binding of Co(III) TMPyP had no obvious effect on the molecular conformation of the protein. Electrostatic force played an important role in the binding due to the opposite charges on porphyrin and the protein.

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