THE METABOLISM OF ANTIGENS IN VIVO: I. PROTEIN ANTIGENS

1964 ◽  
Vol 42 (6) ◽  
pp. 821-832
Author(s):  
M. Richter ◽  
C. Larose ◽  
B. Rose
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Gamma Globulin ◽  
Double Diffusion ◽  
Protein Antigens ◽  
Single Intravenous Injection ◽  
Human Gamma Globulin ◽  
Antigen Interaction

Attempts were made to detect antigenic fragments in the sera or spleens of rabbits given a single intravenous injection of bovine serum albumin, human gamma-globulin, or human serum albumin. The results obtained, using a number of different methods for the detection of antibody–antigen interaction (double diffusion in gel, immunoelectrophoresis, inhibition of hemagglutination), failed to provide any evidence in favor of the presence of antigenic fragments either in the circulation or in the spleen of the experimental animal.

THE METABOLISM OF ANTIGEN IN VIVO: II. AZOPROTEIN

1964 ◽  
Vol 42 (6) ◽  
pp. 833-839
Author(s):  
A. Larose ◽  
B. Rose ◽  
M. Richter
Keyword(s):  
Intravenous Injection ◽  
Experimental Animal ◽  
Gamma Globulin ◽  
Double Diffusion ◽  
Single Intravenous Injection ◽  
Serum Fractions ◽  
Human Gamma Globulin

Experiments were carried out to detect precipitating or non-precipitating antigenic fragments in the serum or spleen of rabbits given a single intravenous injection of arsanil azo – human gamma-globulin. The results, using a number of different methods for the detection of antibody (double diffusion, immunoelectrophoresis, inhibition of hemagglutination by serum fractions obtained by elution of paper electropherograms of the antiserum), failed to provide any evidence for the presence of antigenic fragments either in the circulation or in the spleen of the experimental animal.

High Efficiency Photolabeling of Human Serum Albumin and Human .gamma.-Globulin with [14C]Methyl 4-Azido-2,3,5,6-tetrafluorobenzoate

1995 ◽  
Vol 6 (5) ◽  
pp. 630-634 ◽  
Author(s):  
Raghoottama S. Pandurangi ◽  
Srinivasa R. Karra ◽  
Robert R. Kuntz ◽  
Wynn A. Volkert
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
High Efficiency ◽  
Gamma Globulin ◽  
Human Gamma Globulin

Changes in Protein Adsorption on Self-Assembled Monolayers with Monolayer Order:  Comparison of Human Serum Albumin and Human Gamma Globulin

Langmuir ◽  
2001 ◽  
Vol 17 (24) ◽  
pp. 7645-7651 ◽  
Author(s):  
Stanislaw Petrash ◽  
Tricia Cregger ◽  
Bin Zhao ◽  
Elena Pokidysheva ◽  
Mark D. Foster ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Adsorption ◽  
Gamma Globulin ◽  
Self Assembled Monolayers ◽  
Assembled Monolayers ◽  
Self Assembled ◽  
Human Gamma Globulin ◽  
Order Comparison

UCNP@BSA@Ru nanoparticles with tumor-specific and NIR-triggered efficient PACT activity in vivo

2021 ◽  
Author(s):  
Chao Zhang ◽  
Xusheng Guo ◽  
Xuwen Da ◽  
Yishan Yao ◽  
Haihua Xiao ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Short Wavelength ◽  
Ru Nanoparticles ◽  
Wavelength Absorption ◽  
Tumor Accumulation ◽  
Accumulation Ability

Ru(II)-based photoactivated chemotherapy (PACT) agents are promising, however, the short wavelength absorption (generally < 550 nm) and poor tumor accumulation ability limit their in vivo applications. Herein bovine serum albumin...

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.

scholarly journals Termination of aquired and natural immunological tolerance with specific complexes.

1975 ◽  
Vol 142 (2) ◽  
pp. 312-320 ◽  
Author(s):  
G S Habicht ◽  
J M Chiller ◽  
W O Weigle
Keyword(s):  
T Cells ◽  
B Cells ◽  
Bovine Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Gamma Globulin ◽  
Immunological Tolerance ◽  
Detailed Mechanism ◽  
Thyroid Lesions ◽  
Stimulation Of

It was possible to terminate the induced unresponsive state to bovine serum albumin (BSA) and the natural unresponsive state to autologous thyroglobulin in rabbits (RTg) by immunization with complexes composed of heterologous cross-reacting antibody and the tolerated antigens. The unresponsive state was terminated in rabbits made unresponsive by neonatal injections of BSA and then 3 mo later injected with complexes composed of BSA and guinea pig antihuman serum albumin. This termination was manifested by the presence of anti-BSA plaque-forming cells. Similarly, the natural unresponsive state was terminated in adult rabbits injected with complexes between RTg and guinea pig antibovine thyroglobulin (BTg) in that thyroid lesions and circulating anti-RTg were produced. The results can be best explained by the presence of unresponsive T cells and competent B cells, where the guinea pig gamma globulin (antibody) activates T cells specific for the guinea pig gamma globulin portion of the complexes and thus permits stimulation of B cells competent to the exposed determinants of the tolerated (BSA or RTg) portion of the complexes. The detailed mechanism for the activation of B cells in tolerant animals is discussed.

scholarly journals Separation of antigens by immunological specificity. Use of cellulose-linked antibodies as immunosorbents

1966 ◽  
Vol 101 (3) ◽  
pp. 711-716 ◽  
Author(s):  
RGC Gallop ◽  
BT Tozer ◽  
J Stephen ◽  
H Smith
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gamma Globulin ◽  
High Specificity ◽  
Immunological Specificity

1. Immunosorbents were prepared by coupling activated aminocellulose with the gamma-globulin concentrates of antisera prepared against ovalbumin and human serum albumin. 2. The immunosorbents were low in solubility, but high in capacity for homologous antigens. 3. The high specificity of these immunosorbents was demonstrated by their use in fractionating various mixtures of fluorescent ovalbumin, (131)I-labelled human serum albumin, lysozyme and ribonuclease.

BSA directed-synthesis of biocompatible Fe3O4 nanoparticles for dual-modal T1 and T2 MR imaging in vivo

2017 ◽  
Vol 9 (21) ◽  
pp. 3099-3104 ◽  
Author(s):  
Dong Li ◽  
Minghui Hua ◽  
Kun Fang ◽  
Rong Liang
Keyword(s):  
Bovine Serum Albumin ◽  
Mr Imaging ◽  
Serum Albumin ◽  
Fe3o4 Nanoparticles ◽  
Bovine Serum ◽  
Mild Conditions ◽  
Directed Synthesis ◽  
T1 And T2

Bovine serum albumin-Fe3O4 nanoparticles with undoubted biosafety and robust dual-modal T1 and T2 MR imaging ability were fabricated using a biomineralization approach in a facile way under mild conditions for in vivo MR imaging.

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