Zobrazeno 1 - 10
of 11
pro vyhledávání: '"B C, Weis"'
Publikováno v:
Journal of Biological Chemistry. 270:8952-8957
The expression pattern of mitochondrial carnitine palmitoyltransferase (CPT) enzymes was examined in the developing rat heart. Whereas the specific activity of CPT II increased approximately 3-fold during the first month of life, the profile for CPT
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a8682f14ad39583d963846d9b781cc7
https://doi.org/10.1074/jbc.270.15.8952
https://doi.org/10.1074/jbc.270.15.8952
Publikováno v:
Journal of Biological Chemistry. 269:26443-26448
It has recently been established that rat heart mitochondria contain two isoforms of carnitine palmitoyltransferase I (CPT I), the minor 88-kDa variant being identical to liver CPT I (L-CPT I) and the dominant 82-kDa form resembling the skeletal musc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc2ecc2719368086c6db59a8d7e94c47
https://doi.org/10.1016/s0021-9258(18)47214-6
https://doi.org/10.1016/s0021-9258(18)47214-6
Publikováno v:
Journal of Biological Chemistry. 269:18712-18715
To begin to explore the basis for the tissue-specific expression of mitochondrial carnitine palmitoyltransferase I (CPT I), we focused on three rat tissues (liver, heart, and skeletal muscle) in which the enzyme was known to display very different pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::04a34a17bf1ee6c2babeece0e84a193a
https://doi.org/10.1016/s0021-9258(17)32222-6
https://doi.org/10.1016/s0021-9258(17)32222-6
Publikováno v:
Journal of Biological Chemistry. 268:5817-5822
We report the isolation and characterization of a full-length cDNA encoding rat liver carnitine palmitoyltransferase I (CPT I). Oligonucleotides corresponding to two tryptic peptides derived from the malonyl-CoA/etomoxir-CoA-binding protein of rat li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f5e9c0e73b6cc82a46fe0c6bf4623512
https://doi.org/10.1016/s0021-9258(18)53392-5
https://doi.org/10.1016/s0021-9258(18)53392-5
Autor:
W. F. Cox, J. D. McGarry, B C Weis, Daniel W. Foster, Shyue-Tsong Liao, Keith F. Woeltje, J. G. Schroeder, Victoria Esser
Publikováno v:
Journal of Biological Chemistry. 265:10714-10719
Properties of the carnitine palmitoyltransferase (EC 2.3.1.21) (CPT) enzyme system were compared in isolated mitochondria from a range of tissues in rodents, monkey, and man. Common features were as follows: (a) while membrane-bound, CPT I, but not C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e279d03c734ae42f3af48f4bce02e45d
https://doi.org/10.1016/s0021-9258(18)87005-3
https://doi.org/10.1016/s0021-9258(18)87005-3
Autor:
Michael J. McPhaul, B C Weis, Clive A. Slaughter, Keith F. Woeltje, Daniel W. Foster, Victoria Esser, W. F. Cox, J. D. McGarry, A. Sen
Publikováno v:
Journal of Biological Chemistry. 265:10720-10725
We report the isolation and characterization of a full-length cDNA encoding rat liver carnitine palmitoyltransferase II (CPT II). Beginning with the purified protein CNBr fragments were generated and sequenced. Corresponding oligonucleotides were use
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a505376e2344795ac4cffc8b1c6950c
https://doi.org/10.1016/s0021-9258(18)87006-5
https://doi.org/10.1016/s0021-9258(18)87006-5
Publikováno v:
The Journal of biological chemistry. 269(42)
It has recently been established that rat heart mitochondria contain two isoforms of carnitine palmitoyltransferase I (CPT I), the minor 88-kDa variant being identical to liver CPT I (L-CPT I) and the dominant 82-kDa form resembling the skeletal musc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9b5213dab049f0a5148e7af56563824a
https://pubmed.ncbi.nlm.nih.gov/7929365
https://pubmed.ncbi.nlm.nih.gov/7929365
Publikováno v:
The Journal of biological chemistry. 269(29)
To begin to explore the basis for the tissue-specific expression of mitochondrial carnitine palmitoyltransferase I (CPT I), we focused on three rat tissues (liver, heart, and skeletal muscle) in which the enzyme was known to display very different pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4fd4ae21e2ced1fd8dd19dec0e59e1a8
https://pubmed.ncbi.nlm.nih.gov/8034622
https://pubmed.ncbi.nlm.nih.gov/8034622
Publikováno v:
The Journal of biological chemistry. 268(8)
We report the isolation and characterization of a full-length cDNA encoding rat liver carnitine palmitoyltransferase I (CPT I). Oligonucleotides corresponding to two tryptic peptides derived from the malonyl-CoA/etomoxir-CoA-binding protein of rat li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6495435a5144add2c62598412c1c62b9
https://pubmed.ncbi.nlm.nih.gov/8449948
https://pubmed.ncbi.nlm.nih.gov/8449948
Publikováno v:
Biochimie. 73(1)
Dissection of the mitochondrial carnitine palmitoyltransferase (CPT) enzyme system in terms of its structure/function relationships has proved to be a formidable task. Although no one formulation has gained universal agreement we believe that the wei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0aa133939dc3e4120a61f933a0131cf4
https://pubmed.ncbi.nlm.nih.gov/2031961
https://pubmed.ncbi.nlm.nih.gov/2031961