Three immune globulins in maternal serum and colostrum and newly born calf serum, have been characterized and compared. An examination was made to determine first, which of the maternal serum immune globulins accumulate in the circulation of the calf and secondly, the selectivity of the mammary gland for these proteins compared with the intestinal mucosa of the newly born calf.

By difference in their electrophoretic mobilities three antigenically related immune globulins were isolated from bovine serum.

The immune lactoglobulins in bovine colostrum were qualitatively similar to those in serum. However, marked differences were observed between the relative concentrations in serum and colostrum of the three immune globulins.

An electrophoretically fast immune globulin (C1), present in colostrum at high concentration, was shown to be antigenically similar to an immune globulin (S1) present in the maternal serum at low concentration.

These findings indicate that the mammary gland showed a highly selective preference for, and hence ability to concentrate in, colostrum, the electrophoretically fastest serum immune globulin.

The slowest serum immune globulin and the component with intermediate electrophoretic mobility (S3 and S2 respectively) were both present at high concentration in bovine maternal serum, but were transmitted at different rates into the colostrum, so that the slowest serum immune globulin (S3) was present in the colostrum as a comparatively minor component (C3).

In contrast to the mammary gland, the intestine of the newly born calf (permeable to undegraded protein during the first 24 hours of life) showed no selectivity. Immune globulins showing the three electrophoretic mobilities were absorbed equally readily.

Thus, while the bovine mammary gland showed a highly selective preference for certain electrophoretically different serum proteins, no comparable selectivity was shown by the intestinal mucosa of the newly born calf.

The results emphasize the heterogeneity of bovine immune globulins and show that the calf receives into its circulation from ingested colostrum selected maternal serum immune globulins. This selection of proteins from maternal plasma, for admission to the calf's circulation, occurs within the mammary gland during the formation of colostrum but not during absorption across the calf's intestinal mucosa.

Biophysical and immunological studies on bovine immune globulins with evidence for selective transport within the mammary gland from maternal plasma to colostrum

In the last two decades immunochemists have been concerned with analyzing the interaction between antigen and antibody by physico-chemical means. This approach has been so successful that the tools and methods of chemical physics have become thoroughly integrated into our discipline, We have now entered a new phase in which our attack on longstanding problems is being revitalized and reoriented by a biosynthetic approach. This approach has allowed a concrete attack on such problems as the biological basis of the specificity of antibody and the mechanisms concerned in the synthesis of proteins in general and of antibodies in particular. Our present meeting shows, in all its phases, this new outlook. The study of three-component systems initiated the development of immunochemistry. Determining the amount of antibody, required to neutralize constant quantities of toxin in mixtures injected into animals, led to the first precise measurements of antibody and antigen. However, the complexity of the animal test system, while it permitted the development of a reasonably precise assay method, did not allow a detailed analysis of the kinetics of the system. An early obstacle encountered in the three-component systems arose from the difEculty of isolating macromolecules so that several decades of research were required before purified and defined antigens could be used. This di5culty was overcome some 20 years ago, but a further and greater difficulty of the complex test system remained unresohed. This was that the permeability of membranes, the biological stability of antigens and many other factors play a part in the access of toxin and of antitoxin to the mammalian sites on which the antigens act. Hence detailed analyses, when toxins are used in three-component systems in uivo, are impossible. Further progress in this area has to await the identification of the biochemical principle on which the toxins act. The identification and subsequent purification of the toxin-substrate is needed not only to avoid the complexity of the in uiuo system, but also to permit flexibility of experimentation. However, identification has proved extremely diEcult, and, except in the case of the a-toxin of Clostridium welchiiz02 very little progress has been made. As one consequence of these difEculties, a simplified system, in which only two of the components (antigen and antibody) were involved, engaged the attention of the avant-garde. This led to present knowledge of the nature and specificity of antibody and of the forces which act between antigen and antibody. (See pages 549594,611429,643-673.) While work with toxins in a three-component system was blocked by formidable obstacles, another system of three components-enzyme, anti-

Introduction: immunochemistry of enzymes

The tyrosyl residues of tetanus toxin can be specifically nitrated by tetranitromethane. The introduction of NO2 groups into the toxin molecule is followed by a rapid decrease in toxicity. Although tryptophyl residues are differently involved and some aggregation occurs, these two phenomena do not take any significant part in the toxicity loss. The immunological reactivity in vitro is preserved. However, it is modified when a certain amount of NO2 groups have been introduced. The thus-formed derivative no longer gives a reaction of identity with the native toxin. Furthermore, when a sufficiently large number of NO2 groups have been introduced, two lines of precipitation are seen. Antisera raised in rabbits with a few nitro-derivatives of the toxin exhibit a low avidity. Precipitating power with pure toxin of these antisera is lower than with a normal antitetanus serum. The capability of tetanus toxin to give rise to neutralizing antibodies is not impaired until 33 NO2 groups have been introduced, then it gradually decreases until it finally disappears. Modification of the toxin by nitration allowed us to discriminate three groups of determinants. In particular, the results presented are further substantiated by those given by 3-aminotyrosyl derivatives of tetanus toxin.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1973.tb03115.x

Immunochemistry of Tetanus Toxin

A purification and investigation of tetanus antitoxin

Bien que la vaccination ait entraine une forte regression de la maladie, le tetanos — de par sa gravite meme — pose encore un probleme epidemiologique important, car par negligence ou prevention, beaucoup de personnes arrivent encore a echapper aujourd'hui a l'immunisation active. Il est donc utile de pouvoir apprecier l'etat d'immunite ou la reponse a un procede de vaccination d'une population donnee: le titrage de l'antitoxine dans le sang de l'homme ou des animaux joue un role important. D'une facon generale, pour connaitre le degre de protection antitetanique, on a recours a de nombreuses methodes de laboratoire qui se ramenent finalement a deux grands types: les methodes ≪ in vitro ≫ et les methodes ≪ in vivo ≫. Il est a souligner que le nombre de methodes dont on dispose pour le titrage de l'antitoxine tetanique est considerablement plus faible que dans le cas de la diphterie et que les points principaux d'interet de ces methodes sont le degre de sensibilite, le taux minimum d'antitoxine qui peut etre mesure et le faible volume de serum necessaire a ce test.

Titrage des anticorps antitétaniques

/pdf/the-interaction-of-tetanus-toxin-and-antitoxin-4hqeo5q2r9.pdf

The interaction of tetanus toxin and antitoxin.

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The interaction of tetanus toxin and antitoxin.