scholarly journals Novel Aflatoxin Derivatives and Protein Conjugates

Molecules ◽  
2007 ◽  
Vol 12 (3) ◽  
pp. 641-653 ◽  
Author(s):  
Christian Cervino ◽  
Dietmar Knopp ◽  
Michael Weller ◽  
Reinhard Niessner
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Maldi Ms ◽  
Uv Absorption ◽  
Preparative Hplc ◽  
Two Dimensional ◽  
Protein Conjugates ◽  
Carcinogenic Effects ◽  
Fast Synthesis

Aflatoxins, a group of structurally related mycotoxins, are well known for their toxic and carcinogenic effects in humans and animals. Aflatoxin derivatives and protein conjugates are needed for diverse analytical applications. This work describes a reliable and fast synthesis of novel aflatoxin derivatives, purification by preparative HPLC and characterisation by ESI-MS and one- and two-dimensional NMR. Novel aflatoxin bovine serum albumin conjugates were prepared and characterised by UV absorption and MALDI-MS. These aflatoxin protein conjugates are potentially interesting as immunogens for the generation of aflatoxin selective antibodies with novel specificities.

scholarly journals Investigating resonance energy transfer from protein molecules to van der Waals nanosheets

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 ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Van Der Waals ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Two Dimensional ◽  
Protein Molecules ◽  
2D Nanomaterials

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

Antibodies to Indolealkylamines; Serotonin and Melatonin

1974 ◽  
Vol 52 (3) ◽  
pp. 196-202 ◽  
Author(s):  
Lee J. Grota ◽  
Gregory M. Brown
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molar Ratio ◽  
Double Immunodiffusion ◽  
Protein Conjugates ◽  
Spectrophotometric Data ◽  
Freund’S Adjuvant ◽  
Freund's Adjuvant

Serotonin, N-acetyl serotonin, and 5-methoxy-N-acetyl serotonin (melatonin) were conjugated to bovine serum albumin (BSA) using formaldehyde. The molar ratio of hapten to protein was determined spectrophotometrically. Spectrophotometric data indicated that serotonin and N-acetyl serotonin but not melatonin were conjugated to bovine serum albumin. Selected hapten–protein conjugates were suspended in Freund's adjuvant and injected into rabbits. Antisera were harvested monthly and screened by double immunodiffusion. Immunodiffusion and inhibition tests indicated that antibodies raised to serotonin–BSA reacted with serotonin and 5-methoxytryptamine but failed to cross react with N-acetyl serotonin or melatonin. Inhibition tests indicated that antibodies to N-acetyl serotonin – BSA reacted with N-acetyl serotonin and cross reacted with melatonin but not with serotonin or 5-methoxytryptamine.

scholarly journals Study on the Interaction of Bovine Serum Albumin with Ceftriaxone and the Inhibition Effect of Zinc (II)

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Qiaoli Yue ◽  
Tongfei Shen ◽  
Changna Wang ◽  
Chaohui Gao ◽  
Jifeng Liu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Interactions ◽  
Binding Sites ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Uv Absorption ◽  
Inhibition Effect ◽  
Bsa Binding ◽  
Number Of Binding Sites

The mechanism of the interaction between bovine serum albumin (BSA) and ceftriaxone with and without zinc (II) (Zn2+) was studied employing fluorescence, ultraviolet (UV) absorption, circular dichroism (CD), and synchronous fluorescence spectral methods. The intrinsic fluorescence of BSA was quenched by ceftriaxone in a static quenching mode, which was authenticated by Stern-Volmer calculations. The binding constant, the number of binding sites, and the thermodynamic parameters were obtained, which indicated a spontaneous and hydrophobic interaction between BSA and ceftriaxone regardless of Zn2+. Changes in UV absorption, CD, and synchronous fluorescence spectral data are due to the microenvironment of amide moieties in BSA molecules. In the BSA-ceftriaxone-Zn2+ system, Zn2+ must first interact with ceftriaxone forming a complex, which inhibits BSA binding to ceftriaxone. The present work uses spectroscopy to elucidate the mechanism behind the interaction between BSA and ceftriaxone in the presence and absence of Zn2+. The BSA and ceftriaxone complex provides a model for studying drug-protein interactions and thus may further facilitate the study of drug metabolism and transportation.

Synthesis and Characterization of Hapten-Protein Conjugates for Antibody Production against Cyanogenic Glycosides

2015 ◽  
Vol 78 (7) ◽  
pp. 1408-1413 ◽  
Author(s):  
ISLAMIYAT FOLASHADE BOLARINWA
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Antibody Titer ◽  
Bovine Serum ◽  
Polyclonal Antibodies ◽  
Enzyme Linked Immunosorbent Assay ◽  
Cyanogenic Glycosides ◽  
Protein Conjugates ◽  
Novel Approach ◽  
Cyanogenic Plants

Consumption of cyanogenic plants can cause serious health problems for humans. The ability to detect and quantify cyanogenic glycosides, capable of generating cyanide, could contribute to prevention of cyanide poisoning from the consumption of improperly processed cyanogenic plants. Hapten-protein conjugates were synthesized with amygdalin and linamarin by using a novel approach. Polyclonal antibodies were generated by immunizing four New Zealand White rabbits with synthesized amygdalin-bovine serum albumin and linamarin-bovine serum albumin immunogen. This is the first time an antibody was produced against linamarin. Antibody titer curves were obtained from all the four rabbits by using a noncompetitive enzyme-linked immunosorbent assay. High antibody titer was obtained at dilutions greater than 1:50,000 from both immunogens. This new method is an important step forward in preventing ingestion of toxic cyanogenic glycosides.

scholarly journals Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment

2001 ◽  
Vol 68 (3) ◽  
pp. 483-497 ◽  
Author(s):  
PALATASA HAVEA ◽  
HARJINDER SINGH ◽  
LAWRENCE K. CREAMER
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Whey Protein ◽  
Bovine Serum ◽  
Concentrate Solution ◽  
Polyacrylamide Gel Electrophoresis ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Two Dimensional ◽  
Β Lactoglobulin

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.

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 ◽  
...  
Keyword(s):  
Surface Tension ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Two Dimensional ◽  
Nanostructure Formation
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