The catalase activity of Bact. lactis aerogenes

Cole, Emily; Hinshelwood, Cyril Norman

doi:10.1039/tf9474300266

Cited by 14 publications

(4 citation statements)

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“…Based on observations made of these cultures growing in nutrient broth and on nutrient agar slants, these incubation periods were chosen to obtain ample cell yields with high catalase concentrations. Cole and Hinshelwood (1947) and McCarthy and Hinshelwood (1959) previously reported that catalase content in Bact. lactis aerogenes increased during the logarithmic growth phase, reached a maximum just prior to the stationary growth phase, and then declined exponentially.…”

Section: Resultsmentioning

confidence: 85%

Catalase Activity of Psychrophilic Bacteria Grown at 2 and 30 C1

Frank

Ishibashi

Reid

et al. 1963

Applied Microbiology

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Section: Resultsmentioning

confidence: 85%

Catalase Activity of Psychrophilic Bacteria Grown at 2 and 30 C1

Frank

Ishibashi

Reid

et al. 1963

Applied Microbiology

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“…Decay of enzyme activities in mammalian systems usually follows first order kinetics, for example all enzymes examined in the rat liver decay expentially to basal levels (Schimke, 1g70), but exponential decay in micro-organisms (e.g. Cole & Hinshelwood, 1947) is less common.…”

Section: Discussionmentioning

confidence: 99%

Factors Influencing the Formation and Stability of D-Glucoside 3-Dehydrogenase Activity in Cultures of Agrobacterium tumefaciens

Kurowski¹,

Fensom²,

Pirt³

1975

Journal of General Microbiology

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SUMMARY D-Glucoside 3-dehydrogenase specific acivity in Agrobacterium tumefaciens was maximal towards the end of the exponential growth phase of batch cultures; over go % of the activity disappeared within the next 15 h. Manganese ions, although essential for growth of the organism, strongly repressed D-glucoside 3-dehydrogenase synthesis in sucrose medium but had little effect when the carbon source was methyl a-D-glucoside. D-Glucoside pdehydrogenase activity increased linearly with increasing specific growth rate in chemostat cultures limited by carbon, nitrogen, phosphate or manganese when methyl a-mglucoside was the carbon source. High enzyme activity was found with sucrose as carbon source only when the growth medium was manganese-limited. D-Glucoside 3-dehydrogenase activity disappeared from A. tumefaciens incubated in carbon-and nitrogen-free medium or in nitrogen-free medium containing succinate, but on continued incubation the activity returned and was then stable. The recovery of activity could be prevented by chloramphenicol or erythromycin. Bacteria containing the recovered dehydrogenase activity could not convert sucrose to 3-ketosucrose when oxygen acted as the terminal electron acceptor, but produced 3-ketosucrose at the normal rate in the presence of ferricyanide. D-Glucoside 3-dehydrogenase activity disappeared irreversibly from bacteria incubated in nitrogen-free medium containing sucrose. Loss of activity followed first order kinetics in bacteria taken from nitrogen-, phosphate-or manganeselimited chernostat steady states; an accelerating rate of decay occurred in cells grown under carbon-limitation. 8-HydroxyquinolineY chloramphenicol, erythromycin, 2,4-dinitrophenol and manganese ions could reduce the rate of decay.

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“…This method depends upon the fact that the catalase is itself consumed in decomposing the peroxide. The two measures, c and C, have been shown empirically to be directly proportional (Cole & Hinshelwood 1947).…”

Section: Determination Of Catalase Activitymentioning

confidence: 99%

“…Asparagine deaminase was assayed by determination of the ammonia evolved according to the method of Conway & O'Malley (1942). The actual procedure followed that described by Morrison & Hinshelwood (1949) and McCarthy (1959).…”

Section: Determination Of Asparagine Deaminase Activitymentioning

confidence: 99%

Studies of the enzyme activity of Bact. lactis aerogenes (Aerobacter aerogenes) - I. The effects of cellular disruption on the activities of some typical enzymes

Grant

Hinshelwood

1964

Proc. R. Soc. Lond. B.

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When cells of Bact. lactis aerogenes (Aerobacter aerogenes) are disrupted by exposure for various times ( a ) to benzene, or ( b ) to ultrasonic vibrations the activity of some representative enzyme systems changes according to one of two patterns. In pattern I it rises to a maximum from which it then declines; in pattern II it falls from the start, the rate of fall varying from enzyme to enzyme. β -galactosidase and asparagine deaminase show pattern I and catalase pattern II, whichever method of disruption is used. Non-induced dehydrogenases in ( b ) show pattern I while fully mobilized dehydrogenases show pattern II. All are very rapidly inactivated in ( a ). Discussion of the results suggests that the susceptibility of the enzyme to damage may be a function of its complexity, and that the pattern of inactivation depends upon how far the normal activity is limited by rate of access, this in turn depending partly upon the actual location of the enzyme, which in some cases is in or near the cell surface.

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The catalase activity of Bact. lactis aerogenes

Cited by 14 publications

References 0 publications

Catalase Activity of Psychrophilic Bacteria Grown at 2 and 30 C1

Catalase Activity of Psychrophilic Bacteria Grown at 2 and 30 C1

Factors Influencing the Formation and Stability of D-Glucoside 3-Dehydrogenase Activity in Cultures of Agrobacterium tumefaciens

Studies of the enzyme activity of Bact. lactis aerogenes (Aerobacter aerogenes) - I. The effects of cellular disruption on the activities of some typical enzymes

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