Low-molecular-mass human salivary mucin, MG2: structure and binding of Pseudomonas aeruginosa.
Low-molecular-mass human salivary mucin, MG2: structure and binding of Pseudomonas aeruginosa.
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DOI：
10.1177/10454411930040030901
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
M. Reddy;M. Levine;W. Paranchych
中科院分区：
文献类型：
--
作者：
M. Reddy;M. Levine;W. Paranchych
采用柠康酰化、凝胶过滤和离子交换色谱法从人下颌-舌下唾液（HSMSL）中分离出低分子量的人唾液粘蛋白MG 2。用胰蛋白酶水解后，纯化了两种糖肽。较高分子量的糖肽是高度糖基化的O-连接单元。较低分子量的糖肽糖基化程度较低，含有大部分N-连接单元。用重叠结合法检测了HSMSL组分与铜绿假单胞菌皮利的相互作用。发现皮利与MG 2结合。初步研究表明，这种结合可能涉及蛋白质与蛋白质的相互作用。
Low-molecular-mass human salivary mucin, MG2, was isolated from human submandibular-sublingual saliva (HSMSL) employing citraconylation, gel filtration, and ion-exchange chromatography. Following proteolysis with trypsin, two glycopeptides were purified. The higher molecular weight glycopeptide was highly glycosylated with O-linked units. The lower molecular weight glycopeptide was less glycosylated and contained most of the N-linked units. Interaction between components of HSMSL and pili of Pseudomonas aeruginosa was examined by an overlay binding assay. Pili were found to bind to MG2. Preliminary studies indicated that the binding may involve a protein to protein interaction.