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of 93
pro vyhledávání: '"D W, Foster"'
Autor:
J D McGarry, D W Foster
Publikováno v:
Journal of Lipid Research, Vol 17, Iss 3, Pp 277-281 (1976)
The radioisotopic assay for carnitine first described by Cederblad and Lindstedt (Clin. Chim. Acta. 37:235–543, 1972) and modified by Bøhmer et al (Clin. Chim. Acta. 57:55–61, 1974) has been improved and simplified. As a result, the assay yields
Externí odkaz:
https://doaj.org/article/bfc5974e3999402298e3641345d5c2b3
Publikováno v:
Diabetes. 43:878-883
Autor:
D W, Foster
Publikováno v:
The Mount Sinai journal of medicine, New York. 67(2)
Publikováno v:
Biology of reproduction. 59(6)
Because we had found whole testis from adult rats to be much richer in the messenger RNA for the muscle (M) than for the liver (L) form of mitochondrial carnitine palmitoyltransferase I (CPT I), we sought to determine which cell type(s) accounts for
Publikováno v:
The Journal of biological chemistry. 271(12)
We set out to determine if the cDNA encoding a carnitine palmitoyltransferase (CPT)-like protein recently isolated from rat brown adipose tissue (BAT) by Yamazaki et al. (Yamazaki, N., Shinohara, Y., Shima, A., and Terada, H. (1995) FEBS Lett. 363, 4
Publikováno v:
The Journal of biological chemistry. 269(42)
A cDNA encoding full-length carnitine palmitoyltransferase I (CPT I) from rat liver was expressed in Saccharomyces cerevisiae, a system devoid of endogenous CPT activity. The recombinant enzyme was of the expected size (as deduced from immunoblots),
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
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
Publikováno v:
The Journal of biological chemistry. 269(29)
Rat carnitine palmitoyltransferase (CPT) II was expressed in Saccharomyces cerevisiae. Mitochondrial fractions prepared from the cells displayed high CPT activity and reacted with an antibody to the rat protein on immunoblots, whereas no activity or