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      Biochemical evidence for the reversed polarity of the outer membrane of the bacterial forespore.

      , ,
      The Biochemical journal
      Portland Press Ltd.

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          Abstract

          Measurement of certain membrane-bound enzymic activities was used to study the orientation of the outer membrane of the double-membraned forespore of Bacillus megaterium KM. 2. Adenosine triphosphatase, NADH dehydrogenase and L-malate intact protoplasts, but were readily detected in intact stage II or IV forespores, consistent with reversed polarity of the outer forespore membrane relative to the mother-cell plasma membrane. 3. Measurement of NADH oxidase activity revealed that intact stage III forespores had the same high affinity for NADH as protoplast membrane preparations and protoplast lystates, consistent with ready access of NADH to oxidation sites on the outer forespores membrane. 4. Forespores and protoplasts showed osmometric behaviour in solutions of non-permanent solutes consistent with the presence of an intact permeability barrier in these structures.

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          Author and article information

          Journal
          Biochem. J.
          The Biochemical journal
          Portland Press Ltd.
          0264-6021
          0264-6021
          Dec 1975
          : 152
          : 3
          Article
          10.1042/bj1520561
          1172509
          132169
          526828a8-8553-44f1-ac7d-8a13b4af44df
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