Complex structure of human bronchial mucus glycoprotein.
Complex structure of human bronchial mucus glycoprotein.
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人支气管粘液糖蛋白的复杂结构。
DOI：
10.1111/j.1432-1033.1984.tb08273.x
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
Roussel,P
中科院分区：
文献类型：
--
作者：
Slayter,HS;Lamblin,G;LeTreut,A;Galabert,C;Houdret,N;Degand,P;Roussel,P
通过避免使用还原剂并涉及水提取和Sepharose CL-2B凝胶过滤（在6 M氯化胍中）的方法，从2例患者的痰液中分离人支气管粘液糖蛋白或粘蛋白。化学分析表明约有25-40%的脂质。氨基酸和碳水化合物的分析定量地不同于先前减少粘液后纯化的粘蛋白。这些组分中天冬氨酸和谷氨酸的比例也高于还原痰中的粘蛋白。这些粘蛋白仍然被少量肽污染，但似乎不含二硫键连接的交联蛋白。人支气管粘蛋白在6 M盐酸胍溶液中不形成聚集体，用不同方法进行的电子显微镜观察表明，在200- 1000 nm范围内存在胶束和柔性丝。脱脂除去大部分胶束形式。此后，粘蛋白主要以多分散的柔性延伸线和聚集体的形式出现。
Human bronchial mucus glycoproteins or mucins were isolated from the sputum of two patients by a method avoiding reducing agents and involving water extraction and gel filtration on Sepharose CL‐2B in 6 M guanidinium chloride. The chemical analysis indicated approximately 25–40% lipid. The amino acid and carbohydrate analysis differ quantitatively from that of mucins purified after prior reduction of mucus. These fractions also have a higher proportion of aspartic and glutamic acids than that of the mucins from reduced sputum. These mucins are still contaminated by small amounts of peptides but do not seem to contain disulfide‐attached cross‐linking protein. Human bronchial mucins have a strong tendency to form aggregates except in 6 M guanidinium chloride.Electron microscopy performed with various procedures indicates the presence of both micelles and flexible threads measuring 200–1000nm. Delipidation removes most of the micellar forms. Thereafter mucins appear mainly as polydisperse flexible extended threads and also as aggregates.