منابع مشابه
I63. Triosephosphate Dehydrogenase of Bacterium Coli
THE Booth-Green wet-crushing mill for bacteria has been used previously to prepare a cell-free juice from Bacterium coli in which the components of enzyme systems may be studied. In the present paper a juice has been prepared containing the system which oxidizes 3-phosphoglyceraldehyde. For yeast it has recently been shown that the actual substrate is 1:3-diphosphoglyceraldehyde [Warburg & Chri...
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We use measurements of swimming bacteria in an optical trap to determine fundamental properties of bacterial propulsion. In particular, we directly measure the force required to hold the bacterium in the optical trap and determine the propulsion matrix, which relates the translational and angular velocity of the flagellum to the torques and forces propelling the bacterium. From the propulsion m...
متن کاملThe nutritional properties of killed Bacterium coli.
A previous investigation had shown that the protein and polysaccharide components of enteric bacteria can be separated by heating the cells in a watery suspension at 80" for I h (Roberts, 1949). In continuation of this work the protein of Bacterium coli was fed to rats and guinea-pigs and it was found that if the diet satisfied the peculiar vitamin requirements of the experimental animals, as, ...
متن کاملMultiple lactate dehydrogenase activities of the rumen bacterium Selenomonas ruminantium.
The lactate utilizing strain of Selenomonas ruminantium 5934e was found to contain three lactate dehydrogenase (LDH) activities in sonicated cell extracts. One activity, an NAD dependent L-LDH (L-nLDH) was measured at 15-fold greater levels in extracts of cells grown to mid-exponential phase on glucose compared to cells grown to the equivalent growth stage on DL-lactate. A second nLDH activity ...
متن کاملProperties of lactate dehydrogenase in a psychrophilic marine bacterium.
Lactate dehydrogenase (EC 1.1.1.27) from Vibrio marinus MP-1 was purified 15-fold and ammonium activated. The optimum pH for pyruvate reduction was 7.4. Maximum lactate dehydrogenase activity occurred at 10 to 15 degrees C, and none occurred at 40 degrees C. The crude-extract enzyme was stable between 15 and 20 degrees C and lost 50% of its activity after 60 min at 45 degrees C. The partially p...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1941
ISSN: 0306-3283
DOI: 10.1042/bj0350380