Martin I. Horowitz, Leonore Martinez, V.L.N. Murty
{"title":"牛颌下黏液同质性的免疫化学研究","authors":"Martin I. Horowitz, Leonore Martinez, V.L.N. Murty","doi":"10.1016/0926-6526(64)90008-4","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Immunochemical methods were used to study the homogeneity and immunological relationships of bovine submaxillary mucin preparations isolated according to the methods described by <span>Gottschalk</span><sup>1</sup> and by <span>Pigman</span><sup>2</sup> and their collaborators and disgnated BSM-G (“described by <span>Gottschalk</span>” and BSM-G (“described by <span>Pigman</span>”), respectively.</p></span></li><li><span>2.</span><span><p>2. Antisera suitable for immunodiffusion and immunoelectrophoresis were obtained after intravenous and subcutaneous (with Freunds's adjuvant) injections into rabbits of submaxillary gland extracts and mucins. Antibodies directed against the principal mucin components were produced after injection of BSM-P; this was demonstrated by the quantitative precipitation of sialic acid upon addition of BSM-P to anti-BSM-P.</p></span></li><li><span>3.</span><span><p>3. Neither BSM-G nor BSM-P were homogenous by precipitin-curve analysis. Immunoelectrophoresis showed that BSM-G preparations contained from four to nine components, three of which were glycoproteins. BSM-P did not contain extraneous proteins, but it consisted of at least two glycoproteins. Two of the glycoproteins in BSM-G formed confluent arcs with BSM-P.</p></span></li><li><span>4.</span><span><p>4. Further fractionation<sup>2</sup> BSM-G afforded a fraction which was indistinguishable from BSM-P and which corresponds to approx. 60% of the dry weight of BSM-G.</p></span></li></ul></div>","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 305-317"},"PeriodicalIF":0.0000,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90008-4","citationCount":"12","resultStr":"{\"title\":\"Immunochemical studies of the homogeneity of bovine submaxillary mucins\",\"authors\":\"Martin I. Horowitz, Leonore Martinez, V.L.N. Murty\",\"doi\":\"10.1016/0926-6526(64)90008-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. Immunochemical methods were used to study the homogeneity and immunological relationships of bovine submaxillary mucin preparations isolated according to the methods described by <span>Gottschalk</span><sup>1</sup> and by <span>Pigman</span><sup>2</sup> and their collaborators and disgnated BSM-G (“described by <span>Gottschalk</span>” and BSM-G (“described by <span>Pigman</span>”), respectively.</p></span></li><li><span>2.</span><span><p>2. Antisera suitable for immunodiffusion and immunoelectrophoresis were obtained after intravenous and subcutaneous (with Freunds's adjuvant) injections into rabbits of submaxillary gland extracts and mucins. Antibodies directed against the principal mucin components were produced after injection of BSM-P; this was demonstrated by the quantitative precipitation of sialic acid upon addition of BSM-P to anti-BSM-P.</p></span></li><li><span>3.</span><span><p>3. Neither BSM-G nor BSM-P were homogenous by precipitin-curve analysis. Immunoelectrophoresis showed that BSM-G preparations contained from four to nine components, three of which were glycoproteins. BSM-P did not contain extraneous proteins, but it consisted of at least two glycoproteins. Two of the glycoproteins in BSM-G formed confluent arcs with BSM-P.</p></span></li><li><span>4.</span><span><p>4. Further fractionation<sup>2</sup> BSM-G afforded a fraction which was indistinguishable from BSM-P and which corresponds to approx. 60% of the dry weight of BSM-G.</p></span></li></ul></div>\",\"PeriodicalId\":100172,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides\",\"volume\":\"83 3\",\"pages\":\"Pages 305-317\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6526(64)90008-4\",\"citationCount\":\"12\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926652664900084\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926652664900084","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Immunochemical studies of the homogeneity of bovine submaxillary mucins
1.
1. Immunochemical methods were used to study the homogeneity and immunological relationships of bovine submaxillary mucin preparations isolated according to the methods described by Gottschalk1 and by Pigman2 and their collaborators and disgnated BSM-G (“described by Gottschalk” and BSM-G (“described by Pigman”), respectively.
2.
2. Antisera suitable for immunodiffusion and immunoelectrophoresis were obtained after intravenous and subcutaneous (with Freunds's adjuvant) injections into rabbits of submaxillary gland extracts and mucins. Antibodies directed against the principal mucin components were produced after injection of BSM-P; this was demonstrated by the quantitative precipitation of sialic acid upon addition of BSM-P to anti-BSM-P.
3.
3. Neither BSM-G nor BSM-P were homogenous by precipitin-curve analysis. Immunoelectrophoresis showed that BSM-G preparations contained from four to nine components, three of which were glycoproteins. BSM-P did not contain extraneous proteins, but it consisted of at least two glycoproteins. Two of the glycoproteins in BSM-G formed confluent arcs with BSM-P.
4.
4. Further fractionation2 BSM-G afforded a fraction which was indistinguishable from BSM-P and which corresponds to approx. 60% of the dry weight of BSM-G.
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