Interactions between carbon nanodots with human serum albumin and γ-globulins: The effects on the transportation function

2016 ◽  
Vol 301 ◽  
pp. 242-249 ◽  
Author(s):  
Zi-Qiang Xu ◽  
Qi-Qi Yang ◽  
Jia-Yi Lan ◽  
Jia-Qi Zhang ◽  
Wu Peng ◽  
...  
Author(s):  
Meng-Ying Li ◽  
Chang-Qing Xiao ◽  
Zi-Qiang Xu ◽  
Miao-Miao Yin ◽  
Qi-Qi Yang ◽  
...  

2020 ◽  
Vol 239 ◽  
pp. 122266
Author(s):  
Mochamad Zakki Fahmi ◽  
Denika Liyan Nor Wibowo ◽  
Satya Candra Wibawa Sakti ◽  
Hwei Voon Lee ◽  
Isnaeni

1964 ◽  
Vol 120 (5) ◽  
pp. 967-986 ◽  
Author(s):  
Stewart Sell

The fractional rates of catabolism of isotopically labeled mouse, human, bovine, and guinea pig γ-globulins and human serum albumin were determined in mice and in guinea pigs whose serum γ-globulin and serum albumin levels were elevated by immunization or by injections of exogenous serum proteins. These serum proteins were also followed in mice with different serum γ-globulin levels due to different bacterial environments. The fractional rates of catabolism of the labeled γ-globulins from all species tested were markedly increased in mice with elevated γ-globulins due to immunization; to injections of human, mouse, guinea pig, or rabbit γ-globulins; to exposure to supra normal numbers of bacteria in the environment. Injections of bovine γ-globulin were only partially effective, and injections of human serum albumin had no effect. The γ-globulin catabolic rates were decreased in mice with subnormal serum γ-globulin levels (germfree mice). The catabolic rate of human serum albumin was essentially the same in all mice in spite of differences in serum γ-globulin levels. In contrast, elevation of the serum γ-globulin levels by injections of exogenous γ-globulins or by hyperimmunization with keyhole limpet hemocyanin produced no change in the fractional catabolic rates of the isotopically labeled γ-globulins and labeled albumin in guinea pigs. Thus, a feedback mechanism for the control of the serum γ-globulin concentration appears to be operative in the mouse, but not in the guinea pig. Guinea pigs immunized with antigens in complete Freund's adjuvant or a saline suspension of killed E. coli had an increase in the catabolic rates of all labeled proteins tested including human serum albumin. Evidence is presented that the mechanism of this increase in catabolism is not the same as that seen in mice with elevated serum γ-globulin levels.


2020 ◽  
Vol 49 (1) ◽  
pp. 100-116 ◽  
Author(s):  
Xiao-Xu Ba ◽  
Tian Gao ◽  
Mian Yang ◽  
Peng Jiang ◽  
Feng-Lei Jiang ◽  
...  

1964 ◽  
Vol 120 (4) ◽  
pp. 589-609 ◽  
Author(s):  
John H. Rockey ◽  
Norman R. Klinman ◽  
Fred Karush

Anti-p-azophenyl-ß-lactoside (Lac) antibody has been isolated from equine antiserum by specific precipitation with Lac-HSA (human serum albumin) and Lac-Hy (hemocyanin). Antibody was separated from antigen by chromatography on DEAE cellulose and zone electrophoresis in solvents containing lactose. Six antigenically distinct immunoglobulins have been identified in purified equine anti-Lac antibody: 7S ß2A-globulin, 19S γ-globulin, a 10S γ1 globulin, and three antigenically distinct 7S γ-globulins. The specific hapten-binding activity of the 7S ß2A-antibody and of the 10S γ1-antibody has been demonstrated by equilibrium dialysis and by analytical ultracentrifugation using a combination of schlieren and absorption optics. The 10S γ1-globulin antibody may be representative of a hitherto undescribed class of immunoglobulins.


1961 ◽  
Vol 114 (1) ◽  
pp. 43-50 ◽  
Author(s):  
Tom Webb ◽  
Claude Lapresle

An insoluble specific adsorbent for anti-human serum albumin antibodies was prepared by coupling human serum albumin (H.S.A.) to polystyrene by azo bonds. Rabbit anti-H.S.A. immune serum was passed through a column of the adsorbent. It was shown that different volumes of the immune serum were required for the saturation of the different determinant groups of H.S.A. by their corresponding antibodies. The elution of the anti-H.S.A. antibodies adsorbed on the column was achieved by passing successively through the column an acetate buffer pH 3.0 and a solution of 0.1 N HCl in 0.15 M NaCl. The antibodies were eluted in three different fractions, each of which was composed of γ-globulins only. These three fractions contained different proportions of antibodies of different specificities.


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