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Biomedical subjects

S Shulman

Publications and source records attributed to S Shulman.

At least 163 records · Page 9Linked to original sources
PubMed1977

Subunit structure of 27 S thyroid iodoprotein.

The dissociation of thyroid 27 S iodoprotein by sodium dodecyl sulfate (SDS) and by succinic anhydride was investigated by means of ultracentrifugation and polyacrylamide gel electrophoresis. The iodoprotein obtained from either a human or hog was dissociated into three kinds of subunits (S-19, S-17 and S-12) by SDS treatment. At increased concentrations of SDS, the S-12 subunit was predominant among the dissociation products. The succinylation of 27 S iodoprotein showed essentially the same dissociation pattern as in the case of SDS treatment. The dissociation products of the protein preparations of different animals were qualitatively the same as those of thyroglobulin of the respective animals, confirming the hypothesis that 27 S iodoprotein was composed of two molecules of thyroglobulin. However, the extent of dissociation of 27 S iodoprotein measured by S-12 formation showed higher resistancy of the protein to the dissociating agents than that of thyroglobulin. The contents of sialic acid and hexose as well as iodoamino acids of 27 S iodoprotein were found to be the same as, or not far from, those of thyroglobulin. The dissociability and chemical composition of 27 S iodoprotein was discussed with reference to the subunit structure of the protein.

Anhydrides↗
PubMed1976

Subunit structure of 27 S thyroid iodoprotein.

The dissociation of thyroid 27 S iodoprotein by sodium dodecyl sulfate (SDS) and by succinic anhydride was investigated by means of ultracentrifugation and polyacrylamide gel electrophoresis. The iodoprotein obtained from either a human or hog was dissociated into three kinds of subunits (S-19, S-17 and S-12) by SDS treatment. At increased concentrations of SDS, the S-12 subunit was predominant among the dissociation products. The succinylation of 27 S iodoprotein showed essentially the same dissociation pattern as in the case of SDS treatment. This dissociation products of the protein preparations of different animals were qualitatively the same as those of thyroglobulin of the respective animals, confirming the hypothesis that 27 S iodoprotein was composed of two molecules of thyroglobulin. However, the extent of dissociation of 27 S iodoprotein measured by S-12 formation showed higher resistancy of the protein to the dissociating agents than that of thyroglobulin. The contents of sialic acid and hexose as well as iodoamino acids of 27 S iodoprotein were found to be the same as, or not far from, those of thyroglobulin; The dissociability and chemical composition of 27 S iodoprotein was discussed with reference to the subunit structure of the protein.

Amino Acids↗
PubMed1975

Antibodies to spermatozoa. VI. Comparative studies of sperm-agglutinating activity in groups of infertile and fertile women.

In order to evaluate the significance of sperm antibodies in relation to infertility, studies have been made on both infertile and fertile populations. The infertile population consisted of about 150 couples with long-standing infertility, predominantly of the unexplained type. The fertile population consisted of 78 antepartum women and 35 postpartum women. In all these individuals, sperm antibody was sought by two methods of serum testing, namely, the Kibrick (K-B-M) and the F-D methods of sperm agglutination. In the infertile group, the Kibrich test was positive for 23.1 per cent of the women and 9.6 per cent of the men, whereas the F-D test was positive in 16.4 per cent of the women and 5.0 per cent of the men. In contrast to these values, it was found in the fertile group that the Kibrick test was positive in 2.7 per cent of these women and the F-D test was also positive in 2.7 per cent of them. A number of technical details and precautions have also been emphasized. These principles are intended to minimize the occurence of nonspecific and false-positive results.

Agglutination Tests↗
PubMed1975

Antibodies to spermatozoa. V. Antibody activity in human cervical mucus.

Efforts were made to seek sperm antibody activity in human cervical mucus (C.M.). A procedure of extraction was developed, as well as methods for measurement of total protein and of immunoglubulin level. The antibody testing was done by the Kibrick (K-B-M) and F-D methods. In clear contrast with negative control serum and negative C.M. samples, positive activity could be found in the C.M. extracts from several infertile women. Some of these manifestations were seen as positive K-B-M agglutination, whereas some were seen either as agglutination or immobilization in the F-D test; hence, three kinds of observation can be indicative of sperm antibody in extracts of cervical mucus.

Antibodies↗
PubMed1975

The antigens and autoantigens of the seminal vesicle. II. Immunochemical studies on rabbit vesicular fluid.

Rabbit vesicular fluid (RVF) was shown to contain only one major electrophoretic component. This component, isolated by starch block electrophoresis, was found to have a molecular weight, by determination of sedimentation and diffusion coefficients, of approximately 17,300. This major component was also effective in isoimmunization. Another component, possibly a minor one, had similar antigenic properties. The major component, and the "minor" one also, were found to be highly tissue-specific (that is, accessory glands-specific) and also species-specific. Isoimmunization procedures have led to the production of autoantibodies. No delayed hypersensitivity response or lesions of the accessory glands of reproduction resulted. It was concluded that the major reason no lesions were found was that the rabbit was not able to develop a delayed hypersensitivity type of response to the components of RVF. When rabbit vesicular fluid was ejaculated as part of the seminal plasma, its molecules were still able to induce an autoantibody response by isoimmunization techniques. This was the same as the response induced by rabbit vesicular fluid, itself.

Animals↗