Flammann H T, Weckesser J
J Bacteriol. 1984 Jul;159(1):410-2. doi: 10.1128/jb.159.1.410-412.1984.
The isolate major outer membrane protein from Rhodopseudomonas capsulata St. Louis (ATCC 23782) has a high porin activity in reconstituted phospholipid liposomes. The pore size of the homooligomeric porin with subunits of Mr 33,000 was determined to be about 0.8 nm in radius. Circular dichroism data revealed major portions of the beta structure. Heating of the oligomer resulted in monomer formation, loss of porin activity (60 to 70 degrees C), and change to alpha structure (100 degrees C).
从荚膜红假单胞菌圣路易斯菌株（ATCC 23782）中分离出的主要外膜蛋白在重构的磷脂脂质体中具有较高的孔蛋白活性。该同源寡聚孔蛋白亚基的分子量为33,000，其孔径经测定半径约为0.8纳米。圆二色性数据显示其主要为β结构。该寡聚体加热后会形成单体，丧失孔蛋白活性（60至70摄氏度），并转变为α结构（100摄氏度）。
