scholarly journals Direct evidence for the involvement of domain III in the N-F transition of bovine serum albumin

1986 ◽  
Vol 236 (1) ◽  
pp. 307-310 ◽  
Author(s):  
M Y Khan
Keyword(s):  
Bovine Serum Albumin ◽  
Acid Solution ◽  
Serum Albumin ◽  
Protein Sequence ◽  
Bovine Serum ◽  
Direct Evidence ◽  
Structural Transformations ◽  
The Other ◽  
Ph Range ◽  
Domain Iii

The domain III of bovine serum albumin containing residues 377-582 of the protein sequence was isolated and its behaviour in acid solution was studied. The fragment was found to undergo structural transformations over the pH range 3.5-4.5 known to cause N-F transition in serum albumin. On the other hand, an albumin fragment that was devoid of domain III was unable to exhibit such a transition. These results were consistent with a mechanism where N-F transition involves the separation of domain III from the rest of the albumin starts at about pH 4.3 and is completed at pH 3.5.

Pressure Jump Studies of Proteins. I. Isomerization of Bovine Serum Albumin at Neutral pH

1971 ◽  
Vol 49 (12) ◽  
pp. 1267-1275 ◽  
Author(s):  
D. E. Goldsack ◽  
P. M. Waern
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Change ◽  
Bovine Serum ◽  
Ph Dependence ◽  
Kinetic Studies ◽  
Relaxation Effect ◽  
Pressure Jump ◽  
Relaxation Effects ◽  
Ph Range

Pressure jump kinetic studies of the conformational change occurring in bovine serum albumin in neutral solutions have been carried out over the pH range 6.5–9.5. Two distinct relaxation effects are observed at each pH. The faster relaxation is attributed to binding of the dye to the protein, and the slower relaxation is related to the conformational change occurring in the protein. This slower relaxation effect is pH dependent with a maximum value near pH 8. Detailed analysis of these data leads to a mechanism for the conformational change which indicates that the one form of the protein has an ionizable group with a pK of 8.7 which changes to a pK of 6.7 when the protein undergoes the conformational change. A simple iterative procedure is given for analyzing the pH dependence of a relaxation time constant for a cyclic mechanism involving only one ionizing group controlling the conformational change.

scholarly journals Bovine serum albumin and its behaviour in acid solution

1956 ◽  
Vol 62 (4) ◽  
pp. 569-582 ◽  
Author(s):  
W. F. Harrington ◽  
P. Johnson ◽  
R. H. Ottewill
Keyword(s):  
Bovine Serum Albumin ◽  
Acid Solution ◽  
Serum Albumin ◽  
Bovine Serum

RADIOIMMUNOASSAY OF THYROTROPHIN RELEASING HORMONE (TRH)

1974 ◽  
Vol 77 (3) ◽  
pp. 417-421 ◽  
Author(s):  
T. J. Visser ◽  
R. Docter ◽  
G. Hennemann
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
The Other ◽  
Thyrotrophin Releasing Hormone ◽  
Releasing Hormone ◽  
Double Antibody

ABSTRACT Immunization of rabbits with a conjugate in which L-pGlu-L-His-L-Pro-NH2 (TRH) at the amide side has been coupled to bovine serum albumin (BSA) yielded anti-TRH antibody which was detected by reaction of diluted antiserum with 3H-TRH. A double antibody radioimmunoassay has been developed in which 100 pg unlabelled TRH could be detected. Several analogues tested showed that only pGlu-His-Pro-OMe possessed comparable reactivity, while all the other compounds exhibited very little activity in the assay.

The precipitation of proteins by carboxymethyl cellulose

1975 ◽  
Vol 42 (2) ◽  
pp. 267-275 ◽  
Author(s):  
J. G. Zadow ◽  
R. D. Hill
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Carboxymethyl Cellulose ◽  
Degree Of Substitution ◽  
Maximum Precipitation ◽  
Ph Range ◽  
High Degree ◽  
Β Lactoglobulin

SummaryCarboxymethyl cellulose (CMC) formed insoluble complexes with β-lactoglobulin, bovine serum albumin and Na caseinate. Maximum precipitation of the β-lactoglobulin-CMC complex occurred at pH 3·2, whereas maximum precipitation of the bovine serum albumin-CMC complex and the Na caseinate-CMC complex occurred at pH 2·8. The ratio of CMC to protein for maximum precipitation depended on the protein, being greatest for Na caseinate and least for bovine serum albumin. The percentage of protein precipitated by CMC decreased with increasing ionic strength of the solution, the rate of decrease being least for bovine serum albumin. At a given ionic strength, more protein was precipitated by CMC of high degree of substitution than by CMC of low degree of substitution. The change in pH (ΔpH) occurring on mixing CMC and unbuffered protein solutions, each initially at the same pH, was measured. ΔpH was negative for β-lactoglobulin-CMC mixtures over the pH range 7–2 (minimum at pH 5·5). For bovine serum albumin-CMC and Na caseinate-CMC mixtures, ΔpH was positive between pH 7 and 3·2 (maximum at pH 4·5), zero at pH 3·2 and negative between pH 3·2 and 2·0 (minimum at pH 2·8).

scholarly journals Complex coacervates between bovine serum albumin and anionic polysaccharides: formation and characterization

2021 ◽  
Vol 24 ◽  
Author(s):  
Lorena Oliveira Ferreira ◽  
Monique Barreto Santos ◽  
Edwin Elard Garcia-Rojas
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Initial Study ◽  
Wide Ph Range ◽  
The Fourier Transform ◽  
Ph Range ◽  
The Comparative Study ◽  
Maximum Turbidity

Abstract The comparative study regarding complexes coacervated between Bovine Serum Albumin (BSA) and different polysaccharides, Pectin (PEC) and Gum Acacia (GA), was carried out by evaluating the influence of different ratios (protein:polysaccharide) and sodium chloride (NaCl) concentrations on turbidity and zeta potential. The BSA:PEC complexes were formed in a 10:1 ratio whereas BSA:GA at 3:1. The complexation pH showed different behavior, BSA: PEC complexes exhibited maximum turbidity in a wide pH range (4.9 to 1.5), while BSA: GA had maximum turbidity at pH 3.5. The increase in the concentration of NaCl negatively influenced the complexation. The NaCl concentration of 0.40 mol L-1 suppressed the interaction in BSA:PEC (10:1) and reduced the range formation of BSA:GA (3:1). The Fourier Transform Infrared (FTIR) demonstrated the participation not only of electrostatic interactions, but also of hydrogen bonds in the complexation. This initial study elucidated fundamental aspects about the formation of coacervate complexes between BSA:GA/PEC that assist in directing its application in food products especially, in acidic matrices (pH~4.0) as well as with low concentration of salts, in view of the effect of pH on maximum formation and sensitivity to NaCl. These complexes can be added directly to products in order to add nutritional value or even be used as a new matrix for the encapsulation of bioactive compounds.

The effect of bovine serum albumin-glutaraldehyde and polyethylene glycol polymer on neointimal hyperplasia in rabbit carotid artery anastomosis

2020 ◽  
pp. 088532822096491
Author(s):  
Erturk Karaagac ◽  
Yuksel Besir ◽  
Meltem Kurus ◽  
Orhan Gokalp ◽  
Sahin Iscan ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Carotid Artery ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Neointimal Hyperplasia ◽  
The Other ◽  
Control Group ◽  
Positive Staining ◽  
Staining Score

Objective Since the systemic drugs have been used to reduce the hyperplasic response in the tunica intima, the periadventitial local drug applications to the vascular wall have gained more popularity. In this study, we investigated the effect of bovine serum albumin-glutaraldehyde and polyethylene glycol polymer on neointimal hyperplasia in rabbit carotid artery anastomosis to explore the effects of these two different agents. Methods 21 New Zealand male rabbits were randomly divided into three groups. The carotid artery transection and anastomosis was performed onthe control group. The bovine serum albumin-glutaraldehyde and the polyethylene glycol polymer were applied locally on the other two groups seperatley after transection and anastomosis of the carotid arteries. At the end of 28-day follow-up, the histological and the immunohistochemical results related to neointimal hyperplasia were compared. Results The glue residues were detected in the BSA-glutaraldehyde group, but in the PEG polymer group there was no glue residue. The intima thickness and the intima/media thickness ratio in the control group was significantly higher (p<0.05) than the other groups. These values did not differ significantly between the BSA-glutaraldehyde group and the PEG polymer group (p>0.05). The lumen diameter and the area in the control group were significantly higher (p < 0.05) than the BSA-glutaraldehyde group. These values between the control group and the PEG polymer group did not differ significantly (p>0.05). aSMA-positive staining score in the Control group was found to be significantly lower (p < 0.05) than the BSA-glutaraldehyde and PEG polymer group and the VEGF-positive staining score in the control group was found to be significantly higher (p < 0.05) than the BSA-glutaraldehyde and the PEG polymer group. Conclusions Although the both agents have positive results on neointimal hyperplasia, it would be favorable to use polyethylene glycol polymer, since it does not seem to affect the lumen area and the lumen diameter of the vessel.

scholarly journals Polarization fluoroimmunoassays of progesterone

1994 ◽  
Vol 40 (4) ◽  
pp. 48-51 ◽  
Author(s):  
A. Yu. Kolosova ◽  
S. A. Yeremin ◽  
Ye. M. Gavrilova ◽  
A. M. Yegorov
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Rabbit Antiserum ◽  
The Other ◽  
Model Solutions

A quick reliable homogenous polarization fluoroimmunoassay (PFIA) of progesterone was developed. The assay is carried out with Abbott TDx (USA) polarization fluorometer and it takes 5-7 min to analyze 10 samples by this method. The range of progesterone concentrations determined is 1 to 1000 ng/ml. Fluorescein labeled progesterone-3-carbo- xymethyloxime which was used as tracer (labeled antigen) during analysis has been synthesized and purified. Two types of PFIA were developed: one making use of rabbit antiserum to progesterone-3-carboxymethyloxime conjugated with bovine serum albumin (BSA) or keyhole limpet hemocianin (KLH), in the other antiserum to progesterone-11-hemisuccinate-BSA (or KLH) is used. Different combinations of the tracer and antibodies were used. The sensitivity of heterologous PFIA (with antibodies to immunogen heteroioguos to tracer by structure) was higher than that of homologous PFIA. The test is sufficienctly sensitive and specific. The method is particularly valuable for determination of progesterone in model solutions (using buffer standards).

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