{"title":"α1-糖蛋白结构的研究","authors":"Roland Bourrillon , René Got , Denise Meyer","doi":"10.1016/0926-6526(64)90033-3","DOIUrl":null,"url":null,"abstract":"<div><p>A sialic acid-free glycopeptide preparation was isolated from a proteolytic digest of <em>α</em><sub>1</sub>-glycoprotein (pleuromucoid). By paper electrophoresis at pH 6.4, this fraction showed four zones of same carbohydrate composition but of different amino acid composition and sequence.</p><p>This preparation was submitted to digestion with response, resulting in the release of some free or combined amino acids. After purification by gel filtration on Sephadex G 25, a new glycopeptide was obtained; only a limited number of amino acids were present: aspartic and glutamic acids, threonine, proline, glycine and lysine. By paper electrophoresis at pH 6.4, three zones were identified; their amino acid composition and sequence were determined.</p><p>The structure of the three glycopeptide was found different. Similar results were obtained with orosomucoid.</p><p>The present evidence suggests that the diverse glycopeptide chains of the <em>α</em><sub>1</sub>-glycopeptide don't have all the same consitutition.</p></div>","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 2","pages":"Pages 178-188"},"PeriodicalIF":0.0000,"publicationDate":"1964-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90033-3","citationCount":"13","resultStr":"{\"title\":\"Études sur la structure d'une α1-glycoprotéine\",\"authors\":\"Roland Bourrillon , René Got , Denise Meyer\",\"doi\":\"10.1016/0926-6526(64)90033-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>A sialic acid-free glycopeptide preparation was isolated from a proteolytic digest of <em>α</em><sub>1</sub>-glycoprotein (pleuromucoid). By paper electrophoresis at pH 6.4, this fraction showed four zones of same carbohydrate composition but of different amino acid composition and sequence.</p><p>This preparation was submitted to digestion with response, resulting in the release of some free or combined amino acids. After purification by gel filtration on Sephadex G 25, a new glycopeptide was obtained; only a limited number of amino acids were present: aspartic and glutamic acids, threonine, proline, glycine and lysine. By paper electrophoresis at pH 6.4, three zones were identified; their amino acid composition and sequence were determined.</p><p>The structure of the three glycopeptide was found different. Similar results were obtained with orosomucoid.</p><p>The present evidence suggests that the diverse glycopeptide chains of the <em>α</em><sub>1</sub>-glycopeptide don't have all the same consitutition.</p></div>\",\"PeriodicalId\":100172,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides\",\"volume\":\"83 2\",\"pages\":\"Pages 178-188\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-07-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6526(64)90033-3\",\"citationCount\":\"13\",\"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/0926652664900333\",\"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/0926652664900333","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 13
摘要
从α1-糖蛋白(胸膜黏液)的蛋白水解消化中分离出无唾液酸的糖肽制剂。在pH 6.4条件下，纸电泳结果表明，该组分碳水化合物组成相同，但氨基酸组成和序列不同。该制剂经消化反应后，释放出一些游离或结合的氨基酸。经Sephadex G 25凝胶过滤纯化后，得到一种新的糖肽;只有有限数量的氨基酸存在:天冬氨酸和谷氨酸、苏氨酸、脯氨酸、甘氨酸和赖氨酸。pH 6.4纸电泳鉴定出3个区;测定了它们的氨基酸组成和序列。发现三种糖肽的结构不同。orosomucoid也获得了类似的结果。目前的证据表明，α - 1糖肽的不同糖肽链的结构并不完全相同。
A sialic acid-free glycopeptide preparation was isolated from a proteolytic digest of α1-glycoprotein (pleuromucoid). By paper electrophoresis at pH 6.4, this fraction showed four zones of same carbohydrate composition but of different amino acid composition and sequence.
This preparation was submitted to digestion with response, resulting in the release of some free or combined amino acids. After purification by gel filtration on Sephadex G 25, a new glycopeptide was obtained; only a limited number of amino acids were present: aspartic and glutamic acids, threonine, proline, glycine and lysine. By paper electrophoresis at pH 6.4, three zones were identified; their amino acid composition and sequence were determined.
The structure of the three glycopeptide was found different. Similar results were obtained with orosomucoid.
The present evidence suggests that the diverse glycopeptide chains of the α1-glycopeptide don't have all the same consitutition.
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