Kotarski S F, Linz J, Braun D M, Salyers A A
J Bacteriol. 1985 Sep;163(3):1080-6. doi: 10.1128/jb.163.3.1080-1086.1985.
By analyzing outer membrane proteins of Bacteroides thetaiotaomicron on two-dimensional polyacrylamide gels, we were able to identify 10 protein spots that were associated with growth on chondroitin sulfate but not with growth on glucuronic acid or other monosaccharides. These proteins were distinct from the outer membrane polypeptides that were associated with growth on two other negatively charged polysaccharides, polygalacturonic acid and heparin. Of the 10 protein spots that were associated with growth on chondroitin sulfate, 4 could be detected on immunoblots with antiserum that had been raised against outer membranes from bacteria grown on chondroitin sulfate and then cross-adsorbed with membranes from bacteria grown on glucose. Synthesis of these four proteins appeared to be regulated coordinately with synthesis of the two enzymes that degrade chondroitin sulfate, chondroitin lyase I and II. Although one of the four proteins (Mr 110,000) was similar in molecular weight to the chondroitin lyases, the cross-adsorbed antiserum which detected this outer membrane protein did not cross-react with either of these two enzymes.
通过在二维聚丙烯酰胺凝胶上分析多形拟杆菌的外膜蛋白,我们能够鉴定出10个蛋白点,这些蛋白点与在硫酸软骨素上生长相关,但与在葡萄糖醛酸或其他单糖上生长无关。这些蛋白与在另外两种带负电荷的多糖(聚半乳糖醛酸和肝素)上生长相关的外膜多肽不同。在与硫酸软骨素生长相关的10个蛋白点中,有4个可以在用针对在硫酸软骨素上生长的细菌的外膜产生的抗血清进行免疫印迹时检测到,然后用在葡萄糖上生长的细菌的膜进行交叉吸附。这四种蛋白的合成似乎与降解硫酸软骨素的两种酶(硫酸软骨素裂解酶I和II)的合成协同调节。尽管这四种蛋白中的一种(分子量为110,000)在分子量上与硫酸软骨素裂解酶相似,但检测到这种外膜蛋白的交叉吸附抗血清与这两种酶均无交叉反应。