Orientation of the cell membrane in ghosts and electron transport particles of Mycobacterium phlei.
نویسندگان
چکیده
The chemical and enzymatic composition and the respiratory components of an intact membrane preparation, ghosts from Mycobacterium phlei, were compared to those of the electron transport particles. The ghosts were found to contain 5 to 7% of some of the soluble enzymes associated with the cytoplasm. In contrast, 97% of the total content of cytochromes b, cl + c, and a + a3 was found in the ghost preparation. The content of cytochromes, menaquinone, latent ATPase, and phospholipid was similar in both ghost and electron transport particle preparations. The oxidative activities of the ghosts were similar to or slightly lower than those of the electron transport particles with all substrates tested. Coupled phosphorylation, however, was cryptic with the ghost preparations. Phosphorylation was demonstrable following brief sonication or preincubation of the ghosts with substrates and other components of the phosphate acceptor system. The synthesis of ATP was found to occur within the ghosts. Evidence is presented which suggests that the cell membrane of the ghost is oriented as in the intact cell, whereas the orientation of the membrane in the electron transport particles appears to be inside out.
منابع مشابه
Active Transport of Proline in Membrane Preparations from Mycobacterium phZei*
Active transport of proline was observed in both electron transport particles and cell membrane ghosts from Mycobacterium phlei. The transport of proline was dependent upon substrate oxidation and the presence of Li+ or Na+, but not upon the formation of a high energy phosphorylated intermediate. The requirement for Na+ was different from Na+ coupled transport systems which have been described;...
متن کاملActive transport of proline in membrane preparations from Mycobacterium phlei.
Active transport of proline was observed in both electron transport particles and cell membrane ghosts from Mycobacterium phlei. The transport of proline was dependent upon substrate oxidation and the presence of Li+ or Na+, but not upon the formation of a high energy phosphorylated intermediate. The requirement for Na+ was different from Na+ coupled transport systems which have been described;...
متن کاملEffect of phospholipase A on active transport of amino acids with membrane vesicles of Mycobacterium phlei.
Active transport of proline remained unaffected in phospholipase A-treated electron transport particles from Mycobacterium phlei. However, the steady state level of proline was reduced 50 to 60% in phospholipase A-treated depleted electron transport particles that were devoid of membrane-bound coupling factor-latent ATPase activity. The decrease in the uptake of proline in the phospholipase A-t...
متن کاملEffect of phospholipase A on the structure and functions of membrane vesicles from Mycobacterium phlei.
The phospholipid composition of the electron transport particles and coupling factor-depleted electron transport particles of Mycobacterium phlei are the same, but they differ in contents. The accessibility of partially purified phospholipase A to these membrane phospholipids was found to be different. Treatment of membranes of Mycobacterium phlei with phospholipase A impairs the rate of oxidat...
متن کاملEffect of Phospholipase A on the Structure and Functions of Membrane Vesicles from Mycobacterium phZei*
The phospholipid composition of the electron transport particles and coupling factor-depleted electron transport particles of Mycobacterium phlei are the same, but they differ in contents. The accessibility of partially purified phospholipase A to these membrane phospholipids was found to be different. Treatment of membranes of Mycobacterium phtei with phospholipase A impairs the rate of oxidat...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 248 10 شماره
صفحات -
تاریخ انتشار 1973