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Archibald, Bruce; Morel, François M. M.

doi:10.2307/895187

Cited by 2 publications

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“…Thymidine, TMP and TDP kinase activities were determined using 3 H-thymidine (58.3 mCi/mmol) [28] . Carbamyl phosphate synthetase activity was determined [29] with citrulline quanititated colorimetrically [30] . Aspartate transcarbamylase activity was measured [29] and carbamyl aspartate was quanititated colorimetrically [31] .…”

Section: Enzyme Assaysmentioning

confidence: 99%

Cytotoxicity of Substituted Alkyl-3,4-bis(4-methoxyphenyl)pyrrole-2-carboxylates in L1210 Lymphoid Leukemia Cells

Burnham

Gupton

Krumpe

et al. 1998

Arch. Pharm. Pharm. Med. Chem.

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Section: Enzyme Assaysmentioning

confidence: 99%

Cytotoxicity of Substituted Alkyl-3,4-bis(4-methoxyphenyl)pyrrole-2-carboxylates in L1210 Lymphoid Leukemia Cells

Burnham

Gupton

Krumpe

et al. 1998

Arch. Pharm. Pharm. Med. Chem.

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“…The biosynthetic activity was measured at the pH optimum of 7.5, using the method of Isaac and Holloway [3] in a total volume of 0.75 ml. The reaction was allowed to proceed for 15 min after which time the citrulline produced was estimated by a modification of the method of Archibald [5]. Substrate and extract blanks were used along with standard citrulline solutions covering the range 0-0.5/,gmol citrulline in all assays.…”

Section: Ornithine Transcarbamylase (E C 2133 Arg F)mentioning

confidence: 99%

Expression in Escherichia coli and Pseudomonas aeruginosa of Methylophilus methylotrophus AS1 genes carried on prime plasmids

Kearney

1987

FEMS Microbiology Letters

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SUMMARYPrime plasmids carrying chromosomal fragments of Methylophilus methylotrophus AS1 were transferred to Pseudomonas aeruginosa and Escherichia coli auxotrophs. It was shown that with argF (ornithine transcarbamylase), pyrB (aspartate transcarbamylase) and trpB (tryptophan synthetase, fl-subunit) mutants of E. coli and P. aeruginosa complementation was accompanied by the synthesis of the corresponding M. methylotrophus gene product. These results support the basis of complementation mapping by prime plasmids previously used for M. methylotrophus. The level of expression of the M. methylotrophus genes varied in the two hosts but the regulation of the M. methylotrophus genes under these conditions was less responsive to cultural conditions than their expression in M. methylotrophus. INTRODUCTIONThe lack of auxotrophic mutants of Methylophilus methylotrophus AS1 and the absence of effective chromosome mobilising systems have precluded mapping in this organism by more traditional means. Recent studies ([1] and B. Lyon, P. Kearney, M. Sinclair and B. Holloway, manuscript in preparation), have utilised the pattern of complementation of Pseudomonas aeruginosa and Escherichia coli auxotrophs by prime plasmids and cosmid clones carrying DNA of M. methylotrophus AS1 and M. viscogenes to construct complementation maps of both these methylotrophs. The integrity of mapping data obtained in this way relies on the synthesis of the required gene product which is missing in the recipient. This paper demonstrates that P. aeruginosa and E. coli auxotrophs carrying prime plasmids containing M. methylotrophus genes synthesise the appropriate methylotroph gene products and it examines the regulation of these enzymes.

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Cited by 2 publications

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Cytotoxicity of Substituted Alkyl-3,4-bis(4-methoxyphenyl)pyrrole-2-carboxylates in L1210 Lymphoid Leukemia Cells

Cytotoxicity of Substituted Alkyl-3,4-bis(4-methoxyphenyl)pyrrole-2-carboxylates in L1210 Lymphoid Leukemia Cells

Expression in Escherichia coli and Pseudomonas aeruginosa of Methylophilus methylotrophus AS1 genes carried on prime plasmids

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