Volumetric properties of aqueous solutions of bovine serum albumin, human serum albumin, and human hemoglobin

1987 ◽  
Vol 91 (7) ◽  
pp. 1935-1941 ◽  
Author(s):  
Mohammad. Iqbal ◽  
Ronald E. Verrall
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Human Serum ◽  
Bovine Serum ◽  
Volumetric Properties ◽  
Human Hemoglobin

scholarly journals IMMUNOLOGIC TOLERANCE AFTER SPECIFIC IMMUNIZATION

1964 ◽  
Vol 120 (3) ◽  
pp. 435-447 ◽  
Author(s):  
Marianne M. Dorner ◽  
Jonathan W. Uhr
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Antibody Response ◽  
Serum Albumin ◽  
Human Serum ◽  
Bovine Serum ◽  
The State ◽  
Immunologic Tolerance ◽  
Secondary Antibody

Specific immunologic tolerance to bovine serum albumin (BSA) was induced in approximately one-half of the rabbits that had been primarily immunized and were prepared for a secondary antibody response to BSA. The state of tolerance lasted for several months in the majority of rabbits and was not easily terminated by immunization with human serum albumin followed by BSA.

Glycylglycylglycine as a Synthetic Standard for Serum Protein Determination

1974 ◽  
Vol 20 (1) ◽  
pp. 70-73
Author(s):  
Bernard Klein
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Bovine Serum ◽  
Molar Absorptivity ◽  
Protein Determination ◽  
Synthetic Standard ◽  
Mean Differences

Abstract Glycylglycylglycine was investigated as a reference standard for use in serum protein measurement by the biuret reaction. The tripeptide-biuret solution has a molar absorptivity of 96 at 565 nm, and absorbances at both 550 nm and 565 nm are proportional to concentration. By a manual reference procedure, the 550-nm absorbance of 1.0 g of tripeptide was equivalent to that given by 1.72 ± 0.03 g of human serum albumin or 1.43 ± 0.03 g of bovine serum albumin. By the Technicon N14b automated procedure, the absorbance of 1.0 g of tripeptide at 550 nm was equivalent to that of 1.81 ± 0.02 g of human serum albumin or 1.89 ± 0.03 g of bovine serum albumin. Results for serum protein analyses over the range 4.0 to 9.0 g/dl, when tripeptide or serum albumin was used to prepare calibration curves, showed mean differences of 0.15 g/dl in the manual mode and 0.08 g/dl in the automated mode.

scholarly journals Bovine serum albumin as a resuscitation promoting factor for viable but non-culturable Mycobacterium tuberculosis via the activation of protein kinase A-dependent cellular processes

2021 ◽  
Author(s):  
Yuta Morishige ◽  
Yoshiro Murase ◽  
Kinuyo Chikamatsu ◽  
Akio Aono ◽  
Yuriko Igarashi ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Protein Kinase ◽  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Kinase A ◽  
Bovine Serum ◽  
Vbnc State ◽  
Kinase A

Objective: Mycobacterium tuberculosis (Mtb) H37Ra strain has been reported to rapidly enter the viable but non-culturable (VBNC) state following treatment with an NADH oxidase inhibitor (diphenyleneiodonium [DPI]) and to be resuscitated by fetal bovine serum (FBS). However, the mechanism underlying FBS-induced resuscitation is currently unclear. We tried to reveal the underlying mechanism of FBS-induced resuscitation using M. tuberculosis H37Rv. Methods: First, we evaluated the effect of DPI on culturability, viability and changes of cellular phenotypes toward H37Rv. Secondly, we measured the resuscitation-promoting effects of human serum albumin, egg-white albumin, N-acetyl-L-cysteine, and D-mannitol in DPI-induced VBNC cells, as antioxidative agents have been reported to be key molecules for resuscitation of other microbes. We also evaluated the effect of inhibition of cAMP production and protein kinase A on BSA-induced resuscitation. Results: DPI treatment successfully induced a VBNC state in H37Rv, resulting in a low proportion of culturable cells, loss of acid-fastness and lipid-accumulation but a high proportion of viable cells. Not only FBS but also bovine serum albumin (BSA) alone could resuscitate H37Rv. Contrary to our expectation, only human serum albumin had a similar resuscitative effect to BSA. The inhibition of adenylyl cyclase by SQ22536 did not have a significant effect on resuscitation; however, the inhibition of protein kinase A by H89 strongly suppressed the BSA-induced resuscitation. Conclusion: DPI-induced VBNC Mtb cells may be resuscitated via the activation of protein kinase A-dependent processes through interaction with BSA.

Temperature dependence of certain integrated membrane functions in macrophages

1982 ◽  
Vol 57 (1) ◽  
pp. 115-127
Author(s):  
M Faghihi Shirazi ◽  
N.N. Aronson ◽  
R.T. Dean
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Half Life ◽  
Bovine Serum ◽  
Fluid Phase ◽  
Peritoneal Macrophages ◽  
Turnover Time ◽  
Effect Of Temperature

We have studied the effect of temperature on uptake and degradation of molecules entering mouse peritoneal macrophages by fluid-phase, adsorptive and receptor-mediated pinocytosis, and on degradation of their intracellular proteins. Uptake of [3H]sucrose and uptake and degradation of formaldehyde-treated 125I-labelled human serum albumin and 125I-labelled mannose-bovine serum albumin continued, but were progressively slowed as the temperature decreased from 37 degrees C to 20 degrees C. The uptake and degradation were completely abolished at approximately 15 degrees C. Arrhenius plots for adsorptive and fluid uptake were unilinear, whereas that for receptor-mediated endocytosis showed an inflection point at approximately 20 degrees C. The results did not indicate any distinction between adsorptive and fluid pinocytosis. An ‘intracellular turnover time’ calculated for mannose-bovine serum albumin taken up by the specific route is 19–24 min and this time calculated for human serum albumin is, in contrast, 99 min. Studies of the kinetics of degradation of both endocytosed and endogenous proteins showed similarity in the temperature cut-off of degradation of endocytosed and endogenous long-half-life proteins (congruent to 15 degrees C) and continuance of endogenous short-half-life degradation at much lower temperatures.

scholarly journals Deuteroporphyrin-albumin binding equilibrium. The effects of porphyrin self-aggregation studied for the human and the bovine proteins

1985 ◽  
Vol 229 (1) ◽  
pp. 197-203 ◽  
Author(s):  
M Rotenberg ◽  
R Margalit
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Bovine Serum ◽  
Binding Constants ◽  
Protein Molecule ◽  
Competitive Model ◽  
Phosphate Buffered Saline ◽  
Self Aggregation

The binding equilibrium of deuteroporphyrin IX to human serum albumin and to bovine serum albumin was studied, by monitoring protein-induced changes in the porphyrin fluorescence and taking into consideration the self-aggregation of the porphyrin. To have control over the latter, the range of porphyrin concentrations was chosen to maker dimers (non-covalent) the dominant aggregate. Each protein was found to have one high-affinity site for deuteroporphyrin IX monomers, the magnitudes of the equilibrium binding constants (25 degrees C, neutral pH, phosphate-buffered saline) being 4.5 (+/- 1.5) X 10(7) M-1 and 1.7 (+/- 0.2) X 10(6) M-1 for human serum albumin and for bovine serum albumin respectively. Deuteroporphyrin IX dimers were found to bind directly to the protein, each protein binding one dimer, with high affinity. Two models are proposed for the protein-binding of porphyrin monomers and dimers in a porphyrin system having both species: a competitive model, where each protein molecule has only one binding site, which can be occupied by either a monomer or a dimer; a non-competitive model, where each protein molecule has two binding sites, one for monomers and one for dimers. On testing the fit of the data to the models, an argument can be made to favour the non-competitive model, the equilibrium binding constants of the dimers, for the non-competitive model (25 degrees C, neutral pH, phosphate-buffered saline), being: 8.0 (+/- 1.8) X 10(8) M-1 and 1.2 (+/- 0.6) X 10(7) M-1 for human serum albumin and bovine serum albumin respectively.

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