Mary Boesman

Fetus-specific serum proteins in several mammals and their relation to human α-fetoprotein☆

Abstract 1. 1. Fetal and maternal sera from twelve species of mammals were studied electrophoretically and immunochemically for proteins specific for the fetus. 2. 2. In each species, the fetal serum contained an α-globulin not present in maternal serum. 3. 3. The α-fetoproteins of several species had some of the antigenic determinants found in human α-fetoprotein, although antigenic differences among the α-fetoproteins of different species were also apparent; the α-fetoproteins of the species studied appeared to be analogous proteins. 4. 4. Despite the different types of placentation represented, the placenta of each species appeared to be impermeable to α-fetoprotein.

Passive Transfer of Tuberculin Reactivity in Vitro

A factor capable of effecting passive transfer in vivo of delayed hypersensitivity to tuberculin to recipients that are tuberculin negative was isolated from the dialyzate of disrupted leukocytes of tuberculin-positive individuals. After this factor was incubated with cultures of peripheral leukocytes from tuberculin-negative individuals, the addition of purified protein derivative of tubercle bacilli resulted in leukocyte stimulation similar to that observed after addition of purified protein derivative to leukocytes from tuberculin-positive individuals.

Cellular distribution of serum alpha-foetoprotein in organs of the fetal rat.

THE mammalian foetus synthesizes a serum α-globulin, called α-foetoprotein, which is not found in the adult of the species1–7. Although interspecies structural differences among the α-foetoproteins have been noted4–7, the protein of each species appears to be a homologue of foetuin, or bovine α-foetoprotein5,7. Synthesis of serum α-foetoprotein has been shown to occur in the liver in both the rat foetus8,9 and the human embryo9, and in the yolk sac of the rat9. The cells responsible for this synthesis are not known, however, and it has been suggested that the haematopoietic tissue of the liver may be the site of synthesis8. In the present investigation, the cellular distribution of α-foetoprotein in organs of the rat foetus was investigated by means of the fluorescent antibody method.

Maternofoetal transfer of gamma G immunoglobulins.

BRAMBELL has suggested that the mechanisms which underlie the transmission of antibodies and other plasma proteins from mother to foetus are similar to those which operate in the catabolism of these proteins1. This concept was supported by the observation that maternofoetal transfer of homologous and heterologous γG globulins in the rabbit decreased with the half lives of these proteins1; the species order of decreasing maternofoetal transmission2 arid decreasing half life3 in the rabbit was rabbit > man > ginea-pig > horse > bovine. In this study, the maternofoetal transfer of γG globulin was examined in the mouse, rat and guinea-pig.

Heterogeneity of skin-sensitizing antibodies

Abstract The skin-sensitizing antibodies to bovine milk found in a patient with ataxia-telangiectasia who had no detectable serum γA-globulin were compared after fractionation by DEAE-cellulose chromatography to the skin-sensitizing antibodies to bovine milk and ragweed found in 2 patients who had normal serum concentrations of γG-, γA-, and γM-globulins. All of the skin-sensitizing antibodies to bovine milk in the serum of the patient with no detectable serum γA-globulin could be accounted for in a chromatographic fraction in which only γG-globulin was detected. The skin-sensitizing antibodies to bovine milk and ragweed in the 2 patients with normal serum concentrations of γG-, γA-, and γM-globulins were not restricted to the chromatographic fraction in which only γG-globulin was detected and differences were observed in the elution of the skin-sensitizing antibodies in the three sera studied. Differences in the elution of skin-sensitizing antibodies to bovine milk and ragweed were also observed in the same serum. These data demonstrate that skin-sensitizing antibodies are a heterogeneous group of antibodies with regard to their separation by DEAE-cellulose chromatography and suggest that they may be associated with any one of several immunoglobulins.

Plasma 3S γ1-Globulin: Identity with Erythrocyte Carbonic Anhydrase B

The 3S γ1, 2S γ2, and 0.5S γ2 fractions of human plasma are heterogeneous in protein composition. Although each fraction contained a relatively small amount of protein antigenically related to the immunoglobulin light chains, most of the proteins were unrelated to immunogloublin G or its light chains. Of the 3S γ1-globulins the greater part was immunochemically identical to carbonic anhydrase B and had carbonic anhydrase activity. These findings explain earlier reports of an immunochemical similarity between 3S γ1-globulins and immunoglobulin light chains in spite of marked differences in amino acid and peptide composition between the two. Apparently not all plasma γ-globulins are necessarily immunoglobulins.

Disappearance of intradermally administered plasma immunoglobulins and skin-sensitizing antibodies☆

Abstract Serum antibodies, or reagins, responsible for immediate type hypersensitivity reactions in allergic patients are characterized by their ability to sensitize other individuals on passive transfer; it is generally agreed that an important feature of such sensitization is the firm attachment of these antibodies to the tissues. In the present report, the fixation of antibodies to skin in man was examined by studying the disappearance of skin-sensitizing antibodies, radioiodinated γG-, γA-, and γM-globulins, and radioiodinated albumin from the skin after intradermal injection. Skin-sensitizing antibodies to ragweed disappeared from the intradermal injection site with a half-life of 4.2 to 4.9 days; radioiodinated γG-globulin disappeared from the skin with a half-life of 1.8 ± 0.2 days, radioiodinated γA-globulin had a half-life of 2.4 ± 0.3 days, and radioiodinated γM-globulin had a half-life of 1.7 ± 0.4 days. Radioiodinated albumin disappeared from the intradermal site with a half-life of 1.1 ± 0.2 days. The fractional rate of disappearance of the immunoglobulins was relatively constant to levels as low as 0.1 μg of injected protein, and the fractional disappearance of skin-sensitizing antibodies continued to be constant until the skin-sensitizing antibody activity could no longer be evoked by antigenic challenge. Although the disappearance of skin-sensitizing antibody activity from the intradermal injection site was somewhat slower than that of the radioidinated immunoglobulins, there was no evidence from these data of any firm or irreversible binding of either the reagins or the immunoglobulins to the skin.