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Cytophaga johnsonii

Figure 9-15. Poly I,G-effected separation of the complementary strands of A phage DNA in preparative and analytical CsCl gradients. Upper trace represents the absorbance (260 nm) of the 4-drop (50 tl) fractions (total volume 2.5 ml) measured in a 20 /u.1 microcuvette (2 mm light path). Lower trace represents the microdensitometric tracing of the photograph of the same undiluted material banded in the analytical ultracentrifuge (4°C, 3 mm cell) with added density marker DNA (Cytophaga johnsonii, 1.6945 g/cm dashed line). Peak C contains the DNA strands C, which preferentially bind poly I, G the complementary strands W band under peak W. Symbols dN and NN indicate the positions (densities) of the denatured and native Acbj DNA, respectively. [From Z. Hradecna and W. Szybalski, Virology, 32 633 (1967).]... Figure 9-15. Poly I,G-effected separation of the complementary strands of A phage DNA in preparative and analytical CsCl gradients. Upper trace represents the absorbance (260 nm) of the 4-drop (50 tl) fractions (total volume 2.5 ml) measured in a 20 /u.1 microcuvette (2 mm light path). Lower trace represents the microdensitometric tracing of the photograph of the same undiluted material banded in the analytical ultracentrifuge (4°C, 3 mm cell) with added density marker DNA (Cytophaga johnsonii, 1.6945 g/cm dashed line). Peak C contains the DNA strands C, which preferentially bind poly I, G the complementary strands W band under peak W. Symbols dN and NN indicate the positions (densities) of the denatured and native Acbj DNA, respectively. [From Z. Hradecna and W. Szybalski, Virology, 32 633 (1967).]...
Membrane-bound amylase is synthesized adaptively by a dextranase-producing strain of Cytophaga johnsonii. ... [Pg.371]

Dextran induced the synthesis of a dextranase, which is attached to the outer membrane of the envelope, by an aerobic. Gram-negative bacterium closely related to Cytophaga Johnsonii. The use of proteolytic enzymes, snake venoms, and detergents in solubilizing a dextranase from C.johnsonii has been examined. Chymotrypsin was the only protease that efficiently solubilized the enzyme without destroying the enzymic activity. [Pg.377]


See other pages where Cytophaga johnsonii is mentioned: [Pg.109]    [Pg.264]    [Pg.271]    [Pg.109]    [Pg.264]    [Pg.271]   
See also in sourсe #XX -- [ Pg.263 , Pg.270 ]




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