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Biomedical subjects

H Ambrosius

Publications and source records attributed to H Ambrosius.

At least 127 records · Page 7Linked to original sources
PubMed1976

[Studies on the significance of antigen in the 6-mercapopurine-influenced humoral antibody response in guinea pigs].

The mechanism of suppression of humoral immune response to dinitrophenylated bovine gamma globulin (DNP23-BGG), human serum albumin (HSA), and trinitrophenylated sheep red blood cells (TNP-SRBC) by 6-mercaptopurine (6-MP) was studied in guinea pigs. Following the intradermal application of the antigens emulsified in complete (CFA) or incomplete Freund's adjuvant (IFA) each test animal was given 6-MP, 10 mg/kg/day for 7 days. This treatment resulted in a significant suppression of the anti BGG and anti SRBC agglutinating and complement binding antibody production. The latter was only significantly suppressed if the TNP-SRBC were applied together with CFA and not if TNP-SRBC were given in IFA. The anti DNP and anti HSA antibody formation was not influenced.

Agglutination↗
PubMed1975

[Structural and immunochemical studies of the immunoglobulins of carp (Cyprinus carpio L.) II. Analysis of the subunits].

The 14 S immunoglobulin of the carp (Cyprinus carpio L.) was split into subunits with 0,01 M dithioerythritol. These 5,7 S subunits have a molecular weight of 104 000 and a hexose and hexosamine content of 6.2%. It is likely that the subunits represent HL-half-molecules and not H2L2-monomeres. The values for the molecular of H- and L-chains were 77 000 and 24 000, respectively.

Animals↗
PubMed1975

[Structural and immunochemical studies on the immunoglobulin of carp (Cyprinus carpio L.). III. Valence and affinity of antidinitrophenyl-antibodies].

Carps were immunized with DNP conjugated to human serum albumin, bovine gamma globulin and Brucella abortus. The antibodies were isolated by immunoadsorption. The intrinsic average association constant (Ko) of the antibodies was determined by equilibrium dialysis and ammonium sulphate precipitation employing the monovalent hapten tritiated epsilon-DNP-L-lysine. The tetrameric carp IgM possesses four measurable combining sites per molecule. The affinity (Ko) of the isolated antibodies varied from less than 10(4) M-1 to 2,5-10(5) M-1. The highest determined affinity in the whole serum was 4,4-10(5) M-1. The affinity of antibodies, which was determined in the whole serum was 1,1--1,45 times higher than the affinity of specifically purified antibodies. The selective influence of the antibody isolation procedure was unimportant. The affinity of these IgM antibodies increased twice during the first stage following immunization and did not change significantly over a 25-month period.

Animals↗