Colloidal Dispersion of Chloroplast Material

Milner, Harold W.; Lawrence, Nicole; French, C. S.

doi:10.1126/science.111.2893.633

Cited by 200 publications

(63 citation statements)

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“…(ii) Organisms in the same buffer were put through the pressure cell of Milner, Lawrence & French (1950) at 2 "C and 1-4 x 1oS Pa. Supernatant liquid was kept after centrifuging at 12000 g at 2 "C.…”

Section: Short Communicationmentioning

confidence: 99%

Activities of Anaplerotic Enzymes and Acetyl Coenzyme A Carboxylase in Biotin-deficient Bacillus megaterium

Al-Ssum¹,

White²

1977

Journal of General Microbiology

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Section: Short Communicationmentioning

confidence: 99%

Activities of Anaplerotic Enzymes and Acetyl Coenzyme A Carboxylase in Biotin-deficient Bacillus megaterium

Al-Ssum¹,

White²

1977

Journal of General Microbiology

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“…with a cooled cell containing 2 ml. suspension, or with a bacterial press modified from the apparatus described by Milner, Lawrence & French (1950). The extract was centrifuged at 25,000 g for 20 min.…”

Section: Introductionmentioning

confidence: 99%

The Aliphatic Acylamide Amidohydrolase of Mycobacterium smegmatis: Its Inducible Nature and Relation to Acyl-Transfer to Hydroxylamine

Draper

1967

Journal of General Microbiology

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SUMMARYMycobacterium srnegrnatis NCTC 8 159 grew well in a minimal medium with succinate or acetamide as sole carbon source. Washed bacteria or cell-free extracts hydrolyzed 15 monocarboxylic amides, but not 4 related N-substituted amides. Formamide was the best substrate, followed by n-butyramide. Extracts of bacteria grown on acetamide hydrolyzed formamide about 60 times and butyramide about 20 times as rapidly as bacteria grown on succinate. Other short-chain fatty acylamides were also more rapidly hydrolyzed, but benzamidase activity was not similarly induced by growth on acetamide. Extracts of bacteria grown on succinate transferred acyl groups from propionamide, butyramide and nicotinamide to hydroxylamine, to form hydroxamates. Transferase activity, unlike aliphatic amidase activity, was decreased in extracts of bacteria grown on acetamide. Amidase activity in extracts was purified twofold and freed from transferase activity. Formamidase and butyramidase activities were not separated, and were similarly affected by heat and dithio-bis-nitrobenzoic acid. The amidase was induced by growth on acetate and on butyramide, but not on propionate, butyrate or benzamide, all of which were good growth-substrates. N-methylacetamide and N-acetylacetamide were non-substrate inducers of amidase for bacteria growing on succinate.

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“…Washed suspensions of bacteria, concentrated 10-fold in phosphate buffer, were disrupted using a bacterial press modified from that described by Milner, Lawrence & French (1950). Unbroken bacteria and debris were removed by centrifugation a t l0,OOOg for 20 min.…”

Section: Methodsmentioning

confidence: 99%

The Effect of 8-Azaguanine on the Inducible Oxidation of Guanine by Pseudomonas aeruginosa

Clarke

Meadow

1966

Journal of General Microbiology

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SUMMARYPseudomonas aeruginosa NCTC 8203 was shown to metabolize guanine by deamination to xanthine, which was then oxidized to uric acid and further products. Guanine deaminase activity was present in non-induced bacteria but was 3-4 times greater in guanine-induced bacteria. Xanthine oxidase, and the uric acid oxidizing enzymes, were not found in bacteria grown in a minimal salts medium but were induced by adding guanine or xanthine to the culture medium towards the end of the growth period. When uric acid was added, only the uric acid oxidizing enzymes were induced. Enzyme induction also occurred when washed suspensions of the bacteria were incubated with guanine, xanthine or uric acid in Warburg flasks. 8-Azaguanine was deaminated more rapidly than guanine by non-induced bacteria and the rate was,again greater with guanine-induced bacteria. 8-Azaguanine and 8-azaxanthine were not oxidized and did not induce the synthesis of deaminases or oxidases. 8-Azaguanine and 8-azaxanthine had no effect on the oxidation of guanine, xanthine or uric acid by fully induced bacteria. Equimolar concentrations of 8-azaguanine inhibited adaptation to the oxidation of guanine, xanthine and uric acid when added before the substrates. 8-Azaxanthine, under the same conditions, delayed adaptation to guanine and xanthine oxidation, and completely inhibited adaptation to uric acid. Mutant strains were isolated which were resistant to 1 0 m~-8-azaguanine and 5 m~-8-azaxanthine which completely inhibited growth of the parent strain. Another class of mutants was isolated resistant to 8-azaguanine and not resistant to 8-azaxanthine. Both classes of mutants were indistinguishable from the parent strain in their susceptibility to 8-azaguanine and 8-azaxanthine inhibition of adaptation to purine oxidation.

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Colloidal Dispersion of Chloroplast Material

Cited by 200 publications

References 0 publications

Activities of Anaplerotic Enzymes and Acetyl Coenzyme A Carboxylase in Biotin-deficient Bacillus megaterium

Activities of Anaplerotic Enzymes and Acetyl Coenzyme A Carboxylase in Biotin-deficient Bacillus megaterium

The Aliphatic Acylamide Amidohydrolase of Mycobacterium smegmatis: Its Inducible Nature and Relation to Acyl-Transfer to Hydroxylamine

The Effect of 8-Azaguanine on the Inducible Oxidation of Guanine by Pseudomonas aeruginosa

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