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W O WEIGLE

Publications and source records attributed to W O WEIGLE.

At least 19 recordsLinked to original sources
PubMed1965

THE CATABOLISM OF HOMOLOGOUS AND HETEROLOGOUS 7S GAMMA GLOBULIN FRAGMENTS.

The catabolism of homologous and heterologous 7S gamma globulin fragments obtained by pepsin and papain digestion was studied in rabbits, guinea pigs, and mice. The elimination from the circulation of I* labeled gamma globulin fragments was followed and the urinary excretion of the total and protein-bound I* activity determined. Evidence is presented that the molecular structure responsible for the catabolism of 7S gamma globulin is located in papain fragment III. The elimination of papain fragment III was slow and closely related to the intact gamma globulin, whereas the pepsin fragment and papain fragments I and II were rapidly eliminated and catabolized in all species examined. Prolonged incubation with cysteine altered papain fragment III as shown by a rapid catabolism of a large portion of incubated fragment III within 24 hours after injection. Small amounts of intact RGG and RGG papain fragment III were excreted as protein-bound I* activity in the urine. On the other hand, large amounts of the pepsin fragment and papain fragments I and II of RGG were excreted as protein-bound I* activity in the urine. The possibility of a molecular structure present in papain fragment III, which may be responsible for tubular reabsorption in the kidney, is discussed. The rate of urinary excretion of fragments obtained from RGG was different from that of fragments obtained from gamma globulin of several other species. In general, small amounts of the pepsin fragment and papain fragment III obtained from gamma globulin other than RGG were excreted as protein-bound I* activity. The amounts of fragment I* excreted as protein-bound I* activity depended on the species in which it was injected, as well as the source of the gamma globulin. The rapid catabolism of the pepsin fragment and papain fragments I or II which bear antibody-combining sites suggest that their use for the prophylactic treatment of tetanus and diphtheria in man is limited.

Animals↗
PubMed1965

THE INDUCTION OF AUTOIMMUNITY IN RABBITS FOLLOWING INJECTION OF HETEROLOGOUS OR ALTERED HOMOLOGOUS THYROGLOBULIN.

Experimental autoimmunity was produced in rabbits following injection of altered homologous thyroglobulin. The thyroglobulin was altered by coupling to chemically defined haptens and by heating. With some preparations antibody to native thyroglobulin as well as thyroid lesions were produced. Injections of thyroglobulin coupled to the diazonium derivatives of arsanilic acid and sulfanilic acid were effective when given in either soluble form or incorporated into incomplete Freund's adjuvant) while injections of the same preparations precipitated by alum had relatively little effect on production of antibody or induction of lesions. The injection of native thyroglobulin in soluble form, incorporated into incomplete adjuvant or precipitated by alum usually resulted in production of little or no antibody and only rarely in the formation of lesions. The injection of a heterologous thyroglobulin into rabbits resulted in the production of antibody reacting with both the heterologous and rabbit thyroglobulin, but no thyroid lesions were observed.

Adjuvants, Immunologic↗
PubMed1963

Induction of tolerance to heterologous proteins and their catabolism in C57BL/6 mice.

C57BL/6 mice were rendered tolerant to one or another of 13 soluble protein antigens. Tolerance was induced by a single injection of 20 mg protein within 24 hours after birth. The duration of the unresponsive state was measured and compared with the rates of catabolism of the antigens as determined in adult and new born mice. The data presented fail to show a correlation between the persistence of labeled protein antigen and the duration of tolerance. In several occasions, even an inverse relationship between duration of the unresponsive state and persistence was demonstrated. The results, therefore, strongly indicate that the duration of tolerance is not dependent on the rates of catabolism of the antigens. Several of the commercial protein preparations used in this study contained minor impurities to which the animals were generally not rendered tolerant. By means of diffusion in agar techniques, it was demonstrated that mice injected at birth with a tolerance-inducing dose of antigen would generally not reveal precipitating antibodies to this antigen after the tolerant state had been abolished. A speculative explanation was given in terms of quantitative or qualitative differences of antibodies found in such animals as compared to the immunized control mice. After the 3rd or 4th day of life, newborn mice catabolized I(131)-labeled heterologous proteins at the same rates as adult mice. The apparent slow elimination during the first days of life was, at least in part, the result of retention of nonprotein-bound I(131).

Animals↗
PubMed1962

Termination of acquired immunological tolerance to protein antigens following immunization with altered protein antigens.

Acquired tolerance to BSA in rabbits was terminated following the injection of certain preparations of altered BSA. Injections of Freund's adjuvant containing BSA complexed to anti-BSA, heat-denatured BSA, acetyl-BSA, picryl-BSA, or arsanil-BSA failed to terminate the tolerant state. Except in an occasional tolerant rabbit, injections of these preparations failed to cause the production of precipitating antibody to the altered preparation. Similar results were obtained following injections of alum-precipitated preparations of pepsin-degraded BSA, acetyl-BSA, and picryl-BSA. Injections of Freund's adjuvant containing sulfanil-BSA terminated the tolerant state, but only small amounts of non-precipitating anti-BSA were produced. Injections of Freund's adjuvant containing picryl-acetyl-BSA terminated the tolerant state in two of six rabbits, but again, only small amounts of non-precipitating anti-BSA were produced. Injections of an alum-precipitated preparation of picryl-acetyl-BSA failed to terminate the tolerant state. On the other hand, injections of Freund's adjuvant containing arsanil-sulfanil-BSA terminated the tolerant state in eleven of eleven rabbits and caused the production of precipitating anti-BSA in all nine of the rabbits tested. The tolerant state was terminated also in six of six rabbits injected with an alum-precipitated preparation of arsanil-sulfanil-BSA. Only one of these rabbits produced precipitating anti-BSA. In addition, the injection of BGG-tolerant rabbits with arsanil-BGG, sulfanil-BGG, or arsanil-sulfanil-BGG terminated the tolerant state. These results were discussed in relation to both the clonal selection theory of antibody production and autoimmunity.

Animals↗
PubMed1962

The metabolism of serum proteins in the hen and chick and secretion of serum proteins by the ovary of the hen.

In the chicken, serum gamma globulin (CGG) is preferentially transferred by the follicular epithelium of the ovary to the developing ova. The concentration of gamma globulin in the yolk of the unfertilized egg is many times the concentration of chicken serum albumin (CSA). This transfer occurs largely during the 4 to 5 days preceding ovulation when the growth of the ovum is most rapid. Thus, in the chicken, the follicular epithelium of the ovary serves the same purpose in the passive immunization of offspring as does the acinar epithelium of the udder in ungulates and the extraembryonic membranes in rabbits and man. The amount of gamma globulin synthesis by the chick is low during the first 2 weeks of life and is associated with low levels of serum gamma globulin. By the end of the 1st month of life, the level of serum gamma globulin increases, presumably reflecting an increased rate of synthesis. In the adult hens the half-life of I(131)-labeled CSA is 66 hours and that of I(131)-labeled CGG, 35 hours, while in the newly hatched chick for I(131)-labeled CSA it is 42 hours and for I(131)-labeled CGG, 72 hours. Thus, this species shows a gamma globulin sparing in the first days of life, as do most mammalian species.

Animals↗