Zobrazeno 1 - 10
of 10
pro vyhledávání: '"N M, Broadway"'
Autor:
N. M. Broadway, E.David Saggerson, Nigel Turner, Richard J. Pease, Graeme M. Birdsey, Majid Shayeghi
Publikováno v:
Biochemical Journal. 370:223-231
Liver microsomal fractions contain a malonyl-CoA-inhibitable carnitine acyltransferase (CAT) activity. It has been proposed [Fraser, Corstorphine, Price and Zammit (1999) FEBS Lett. 446, 69—74] that this microsomal CAT activity is due to the liver
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3f3d4a3f8145c0d404047fbc6788e74
https://doi.org/10.1042/bj20021269
https://doi.org/10.1042/bj20021269
Autor:
E D Saggerson, Nigel Turner, Graeme M. Birdsey, N. M. Broadway, Majid Shayeghi, Richard J. Pease
Publikováno v:
Biochemical Society Transactions. 29:267-271
Liver microsomes contain two carnitine acyltransferase activities. One of these has properties closely corresponding to those of 88 kDa mitochondrial carnitine palmitoyltransferase-1 (CPT-1). Antisera against CPT-1 cross-react with an 88 kDa microsom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::faef1c28ad1abb9209b1119f0320d8eb
https://doi.org/10.1042/bst0290267
https://doi.org/10.1042/bst0290267
Autor:
E D Saggerson, N. M. Broadway
Publikováno v:
Biochemical Journal. 322:435-440
We have investigated the extent to which membrane environment affects the catalytic properties of the malonyl-CoA-sensitive carnitine acyltransferase of liver microsomal membranes. Arrhenius-type plots of activity were linear in the absence and prese
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b28a9449ad2c950fd4f75ac3fbd760b3
https://doi.org/10.1042/bj3220435
https://doi.org/10.1042/bj3220435
Autor:
N. M. Broadway, E D Saggerson
Publikováno v:
Biochemical Journal. 310:989-995
Conditions have been developed for the solubilization of hepatic microsomal carnitine acyltransferase activity in good yield, with excellent long-term stability and with retention of malonyl-CoA sensitivity. Solubilized microsomal carnitine acyltrans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad097385ad3c035806b3a393984321e7
https://doi.org/10.1042/bj3100989
https://doi.org/10.1042/bj3100989
Autor:
E.David Saggerson, N. M. Broadway
Publikováno v:
FEBS Letters. 371:137-139
The sulphonylureas glibenclamide and tolbutamide inhibited carnitine acyltransferase activities in rat liver microsomes. Glibenclamide was a more potent inhibitor than tolbutamide. The effect of tolbutamide on the malonyl-CoA-inhibitable transferase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ada3d284d8d6fd688010f6bd4105d939
https://doi.org/10.1016/0014-5793(95)00877-c
https://doi.org/10.1016/0014-5793(95)00877-c
Publikováno v:
Current Views of Fatty Acid Oxidation and Ketogenesis ISBN: 9780306462009
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a85cdd1bc0f73b0ea2a7abb66db63b9a
https://doi.org/10.1007/0-306-46818-2_6
https://doi.org/10.1007/0-306-46818-2_6
Publikováno v:
Biochemical Society transactions. 29(Pt 2)
Liver microsomes contain two carnitine acyltransferase activities. One of these has properties closely corresponding to those of 88 kDa mitochondrial carnitine palmitoyltransferase-1 (CPT-1). Antisera against CPT-1 cross-react with an 88 kDa microsom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::01e76cf3b31b06ece101915f931c830e
https://pubmed.ncbi.nlm.nih.gov/11356165
https://pubmed.ncbi.nlm.nih.gov/11356165
Publikováno v:
Advances in experimental medicine and biology. 466
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::596c94a177aa62b0306eebe649bb805d
https://pubmed.ncbi.nlm.nih.gov/10709628
https://pubmed.ncbi.nlm.nih.gov/10709628
Autor:
E D Saggerson, N. M. Broadway
Publikováno v:
Biochemical Society transactions. 23(3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::615334ba1f6b96ae2bff28afd5107f7f
https://pubmed.ncbi.nlm.nih.gov/8566389
https://pubmed.ncbi.nlm.nih.gov/8566389
Autor:
Patti A. Quant, David Saggerson, Elizabeth M. C. Fisher, Sharon J. Nicholson, Josephine Peters, Carole D. Nickols, Mahmoud Naase, N. M. Broadway, Abi S. Witherden, Joanne E. Martin, Demet Araç, Carol Lascelles, Majid Hafezparast, Edwin Cooper, C S Baker, Simon T. Ball, Stephen Gokhale
Publikováno v:
Scopus-Elsevier
Low blood sugar levels are a well-known cause of severe illness and often death in newborn humans, especially those that are small for age. Few of the causes of neonatal hypoglycemia are known, and many remain to be found. We describe a novel mouse m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8ccabccc25cc3037025569fdad54460
http://www.scopus.com/inward/record.url?eid=2-s2.0-0036017942&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0036017942&partnerID=MN8TOARS