The major outer membrane protein patterns of 45 strains of human origin were compared with that of K12 by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Preparations of the former strains contained between two and five major bands in the molecular weight range between 30000 and 42000. The patterns were very heterogeneous with respect to the numbers and electrophoretic mobilities of the major outer membrane protein bands. In all cases the fastest moving band was characterized as a protein similar to the protein of strain K12 as it was partially degraded by trypsin and reacted specifically with antiserum against the purified protein in a gel immuno-radioassay. All the other major outer membrane proteins are related to the and proteins (the porins) of strain K12 as they were peptidoglycan-associated and reacted with antisera against the purified and/or proteins.


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