scholarly journals Stepwise cleavage of rabbit immunoglobin G by papain and isolation of four types of biologically active Fc fragments

1969 ◽  
Vol 112 (3) ◽  
pp. 343-355 ◽  
Author(s):  
Sayaka Utsumi
Keyword(s):  
Guinea Pig ◽  
Immunoglobulin G ◽  
Hinge Region ◽  
Biologically Active ◽  
Antigenic Structure ◽  
Antigenic Determinants ◽  
Fc Fragment ◽  
Pig Skin ◽  
Neutral Ph ◽  
Immunoglobin G

Four types of Fc fragments of different sizes were isolated by papain treatment of rabbit immunoglobulin G under various conditions and by subsequent chromatographic procedures. 1. Brief digestion at neutral pH without reduction produced a molecule in which the Fab and Fc fragments were still linked by a pair of labile disulphide bridges, and the Fc fragment released by cleaving these bonds, called 1Fc fragment, contained a portion of the ‘hinge’ region including an interchain disulphide bridge. Both complement-binding and guinea-pig skin-binding activities were retained by this fragment, which had mol. wt. 48000. 2. Prolonged digestion at neutral pH of immunoglobulin G whose labile inter-heavy-chain disulphide bridges had been reduced removed the ‘hinge’ region, giving mFc fragments (mol. wt. 46000), which lacked the capacity to bind guinea-pig skin but retained the antigenic as well as the complement-binding activities of 1Fc fragment completely. 3. Digestion at pH5·0 yielded a smaller fragment, sFc (mol. wt. 40000), which was no longer able to bind complement. Though the antigenic structure was intact, sFc fragment was curiously unable to precipitate with antibodies to the N-terminal determinants. 4. Fragment stFc (mol. wt. 25000), representing the C-terminal portion of Fc fragment, was formed from all the larger fragments by digestion at pH4·5. Only the C-terminal antigenic determinants were retained by stFc fragment.

scholarly journals The controlling effect of carbohydrate in human, rabbit and bovine immunoglobulin G on proteolysis by papain

1969 ◽  
Vol 111 (4) ◽  
pp. 473-478 ◽  
Author(s):  
R. B. Payne
Keyword(s):  
Immunoglobulin G ◽  
Polypeptide Chain ◽  
Initial Rate ◽  
Hinge Region ◽  
Fc Fragment ◽  
Rabbit Igg ◽  
Initial Cleavage ◽  
Bovine Immunoglobulin ◽  
Hydrolysis Of ◽  
Papain Digestion

About two-thirds of the hexose of human and rabbit immunoglobulin G (IgG) was located in the Fc fragment and one-third in the ‘hinge’ region of the γ (heavy) polypeptide chain at the junction of the Fab and Fc fragments. In contrast, bovine IgG contained more hexose in the ‘hinge’ region than in the Fc fragment. The initial cleavage of susceptible IgG molecules into Fab and Fc fragments by papain under the conditions given by Porter (1959) had reached completion after digestion for 2hr., though bovine IgG was digested somewhat more slowly than human or rabbit IgG. The release of ‘hinge’ peptides from human and rabbit IgG had also reached completion by 2hr., but was slower from bovine IgG and continued for several hours longer. Since bovine IgG molecules contained on the average a greater amount of hexose in the ‘hinge’ region, carbohydrate on this part of the γ-chain may influence not only the initial rate of enzymic hydrolysis into Fab and Fc fragments, but also, and to a greater extent, the rate of further limited hydrolysis of the N-terminal regions of the Fc fragment. The presence of carbohydrate in the ‘hinge’ region does not appear to account for the resistance of some IgG molecules to papain digestion and of some Fc fragments to N-terminal degradation.

scholarly journals Cutaneous lipogenesis: precursors utilized by guinea pig skin for lipid synthesis

1971 ◽  
Vol 12 (3) ◽  
pp. 347-360
Author(s):  
VICTOR R. WHEATLEY ◽  
LEONARD T. HODGINS ◽  
WILLIAM M. COON ◽  
MUTUKUMARA KUMARASIRI ◽  
HAROLD BERENZWEIG ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Lipid Synthesis ◽  
Pig Skin

Final Report of the Safety Assessment of Kojic Acid as Used in Cosmetics

2010 ◽  
Vol 29 (6_suppl) ◽  
pp. 244S-273S ◽  
Author(s):  
Christina L. Burnett ◽  
Wilma F. Bergfeld ◽  
Donald V. Belsito ◽  
Ronald A. Hill ◽  
Curtis D. Klaassen ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Safety Assessment ◽  
Expert Panel ◽  
Kojic Acid ◽  
Tumor Promotion ◽  
Final Report ◽  
Cosmetic Products ◽  
Pig Skin ◽  
Animal Data ◽  
Skin Lightening

Kojic acid functions as an antioxidant in cosmetic products. Kojic acid was not a toxicant in acute, chronic, reproductive, and genotoxicity studies. While some animal data suggested tumor promotion and weak carcinogenicity, kojic acid is slowly absorbed into the circulation from human skin and likely would not reach the threshold at which these effects were seen. The available human sensitization data supported the safety of kojic acid at a use concentration of 2% in leave-on cosmetics. Kojic acid depigmented black guinea pig skin at a concentration of 4%, but this effect was not seen at 1%. The Cosmetic Ingredient Review (CIR) Expert Panel concluded that the 2 end points of concern, dermal sensitization and skin lightening, would not be seen at use concentrations below 1%; therefore, this ingredient is safe for use in cosmetic products up to that level.

Phospholipids (PL) in the Arthus reaction sites induced in guinea-pig skin

1994 ◽  
Vol 8 (1) ◽  
pp. 84
Author(s):  
T. Tachibana ◽  
S. Taniguchi ◽  
S. Imamura
Keyword(s):  
Guinea Pig ◽  
Arthus Reaction ◽  
Pig Skin

scholarly journals Transfer of diclofenac sodium across excised guinea pig skin on high-frequency pulse iontophoresis. I. Equivalent circuit model.

1990 ◽  
Vol 38 (4) ◽  
pp. 1019-1021 ◽  
Author(s):  
Tamotsu KOIZUMI ◽  
Masawa KAKEMI ◽  
Kazunori KATAYAMA ◽  
Hirohiko INADA ◽  
Kazuyoshi SUDEJI ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Equivalent Circuit ◽  
High Frequency ◽  
Diclofenac Sodium ◽  
Equivalent Circuit Model ◽  
Circuit Model ◽  
Pig Skin ◽  
Frequency Pulse

The role of the skin in rabies infection

1926 ◽  
Vol 22 (10) ◽  
pp. 1179-1179
Author(s):  
K. Khalyapin
Keyword(s):  
Virus Infection ◽  
Guinea Pig ◽  
Rabies Virus ◽  
Anatomical Features ◽  
Pig Skin ◽  
Highly Sensitive ◽  
Rabies Virus Infection

The author verified by experiment that the guinea pig skin is an organ highly sensitive to the rabies virus - infection with rabies through the skin is very easy, which the author puts in connection with its anatomical features (a rich network of nerves).

scholarly journals Immunochemical characterization of human plasma fibronectin

1980 ◽  
Vol 191 (3) ◽  
pp. 719-727 ◽  
Author(s):  
M Vuento ◽  
E Salonen ◽  
K Salminen ◽  
M Pasanen ◽  
U K Stenman
Keyword(s):  
Human Plasma ◽  
Antigenic Structure ◽  
Antigenic Determinants ◽  
Proteolytic Degradation ◽  
Plasma Fibronectin ◽  
Native Protein ◽  
Covalent Interaction ◽  
Antigenic Activity ◽  
Haemagglutinating Activity

Human plasma fibronectin has been purified by a non-denaturing affinity chromatography procedure [Vuento & Vaheri, (1979) Biochem.J. 183, 331–337], and antisera have been raised by immunizing rabbits with the native protein. The antisera reacted strongly with native fibronectin, but only weakly with reduced and alkylated fibronectin or with heat-denaturated fibronectin. Denaturation also affected the haemagglutinating and gelatin-binding activities of fibronectin and increased its susceptibility to proteolytic degradation. The antisera reacted with fragments of fibronectin obtained by proteolysis with plasmin. Large fragments (mol.wt. 180000–200000), lacking the region harbouring the interchain disulphide bridges but containing the sites responsible for gelatin-binding and haemagglutinating activity, showed as intense a reaction with the antisera as intact fibronectin. Smaller peptides showed a weaker reaction. All fragments tested showed sensitivity to denaturation in their reaction with the antisera. The results were interpreted as showing that: (1) native fibronectin has an ordered conformation that is easily perturbed by denaturation; (2) most of the antigenic determinants of the protein are dependent on conformation; (3) the region of the fibronectin molecule containing the interchain disulphide bridges has only few antigenic determinants; and (4) covalent interaction of the two subunits does not contribute to the antigenic structure recognized by rabbit antisera. The observed correlation between the antigenic activity and a structural and functional intactness of fibronectin suggests that the antibodies to native fibronectin could be used as a conformational probe in studies on this protein.

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