Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Iain A. Borthwick"'
Publikováno v:
European Journal of Biochemistry. 129:615-620
5-Aminolaevulinate synthase from chick-embryo liver mitochondria has, for the first time, been purified to homogeneity in its native non-degraded form by molecular sieve chromatography, chromatofocusing and affinity chromatography. The enzyme has a m
Publikováno v:
Journal of Biological Chemistry. 268:1109-1117
The housekeeping enzyme 5-aminolevulinate synthase (ALAS) regulates the supply of heme for respiratory cytochromes. Here we report on the isolation of a genomic clone for the rat ALAS gene. The 5'-flanking region was fused to the chloramphenicol acet
Autor:
Gopesh Srivastava, Iain A. Borthwick, Brian K. May, D. J. Maguire, William H. Elliott, Cornelis J. Elferink
Publikováno v:
Journal of Biological Chemistry. 262:3988-3992
Reports to date have led to the conclusion that there are isozymes for 5-aminolevulinate synthase in the liver and erythroid tissue of chicken. Indeed, the existence of a multigene family for chicken 5-aminolevulinate synthase has been proposed. We f
Autor:
Cornelis J. Elferink, D. J. Maguire, Gopesh Srivastava, Brian K. May, J. F B Mercer, M. J. Bawden, Iain A. Borthwick
Publikováno v:
Journal of Biological Chemistry. 263:5202-5209
cDNA clones for rat liver 5-aminolevulinate synthase have been isolated and used to examine mRNA levels in different rat tissues. Northern hybridization analysis of total RNA from various rat tissues showed the presence of a single 5-aminolevulinate
Publikováno v:
Biochemical and Biophysical Research Communications. 110:23-31
Following the recent demonstration [Borthwick, I.A., Srivastava, G., Brooker, J.D., May, B.K. and Elliott, W.H. (1982) Eur. J. Biochem. in press] that chick embryo liver mitochondrial δ-aminolevulinate synthase has a minimum molecular weight of 68,0
Autor:
Brian K. May, W.H. Elliott, Adrienne R. Day, Peter L. Wigley, Gopesh Srivastava, Deborah J. Maguire, Iain A. Borthwick
Publikováno v:
Nucleic Acids Research. 14:1379-1391
5-Aminolevulinate synthase, the first and rate-controlling enzyme of heme biosynthesis, is regulated in the liver by the end-product heme. To study this negative control mechanism, we have isolated the chicken gene for ALA-synthase and determined the
Autor:
Brian K. May, Gopesh Srivastava, J.D. Brooker, John C. Wallace, Iain A. Borthwick, W.H. Elliott
Publikováno v:
Biochemical and Biophysical Research Communications. 117:344-349
Pulse labelling studies in chick embryo livers show that hemin prevents the transfer of drug induced pre-δ-aminolevulinate synthase from the cytosol into the mitochondria, leading to an accumulation of precursor in the cytosol. No effect of hemin wa
Autor:
Gopesh Srivastava, J.D. Brooker, Brian K. May, Byron A. Pirola, Andrew A. Hobbs, Iain A. Borthwick, W.H. Elliott
Publikováno v:
European journal of biochemistry. 144(1)
Hepatic 5-aminolevulinate synthase was induced in chick embryos by administration of the porphyrinogenic drugs 2-allyl-2-isopropylacetamide and 3,5-diethoxycarbonyl-1,4-dihydrocollidine. A cDNA library was constructed from drug-induced liver mRNA and
The proposed mechanism by which hepatic ALV-synthase mitochondrial levels are regulated is outlined in Fig. 2. ALV-synthase catalyzes the first and rate-limiting step in the heme pathway and is normally present in low amounts. A cytosolic, regulatory
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::90f55fee1c1d6d37586ea7b31388f841
https://doi.org/10.1016/b978-0-12-152828-7.50008-1
https://doi.org/10.1016/b978-0-12-152828-7.50008-1
Publikováno v:
European journal of biochemistry. 136(2)
The induction of cytochrome P450 in chick embryo liver has been studied using three different porphyrinogenic drugs, 2-allyl-2-isopropylacetamide, 3,5-diethoxycarbonyl-1,4-dihydrocollidine and phenobarbital. Pulse-labelling studies have shown that fo