Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Luisa Raijman"'
Publikováno v:
Biochemical Journal. 292:241-247
Information on the regulation of urea synthesis in vivo was obtained by examining the relationship between ureagenesis in vivo, citrulline synthesis in vitro, and two factors currently hypothesized to exert short-term regulation of this pathway: the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13e0f706da696117bfb85f7fc557dfa7
https://doi.org/10.1042/bj2920241
https://doi.org/10.1042/bj2920241
Publikováno v:
Biochemical Journal. 282:173-180
Previous studies using intact rat liver mitochondria have shown that the soluble matrix enzymes carbamoyl-phosphate synthase (ammonia) (CPS) and ornithine carbamoyltransferase (OCT) display some kinetic properties which would not be observed if they
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b04a8322418185d2602e9f881c7c776
https://doi.org/10.1042/bj2820173
https://doi.org/10.1042/bj2820173
Publikováno v:
Technological and Medical Implications of Metabolic Control Analysis ISBN: 9780792361893
The pathway of urea synthesis of mammalian liver has proved to be an excellent model for the investigation of the intracellular organization of soluble enzymes. Studies of the behaviour and regulation of the enzymes of this pathway in situ (reviewed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0e1d2c5040959f882c371e82eec10327
https://doi.org/10.1007/978-94-011-4072-0_22
https://doi.org/10.1007/978-94-011-4072-0_22
Publikováno v:
Biochemical Journal. 245:375-379
Mitochondrial water spaces were determined by centrifugal filtration, by using 3H2O and [14C]-sucrose, -mannitol, -inulin and -dextran. The volume (in microliter/mg of mitochondrial protein) of each of the spaces was inversely proportional to the amo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff4e240e12e96d527dc146372f25e6e4
https://doi.org/10.1042/bj2450375
https://doi.org/10.1042/bj2450375
Autor:
Luisa Raijman, Chia-Wei Cheung
Publikováno v:
Archives of Biochemistry and Biophysics. 209:643-649
It has been proposed that arginine may stimulate urea synthesis in vivo by activating amino acid acetyltransferase and thereby increasing the mitochondrial content of acetylglutamate ( K. Shigesada, K. Aoyagi, and M. Tatibana, 1978 , Eur. J. Biochem.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82de8833a26e74fb2f34d5961c14ecc8
https://doi.org/10.1016/0003-9861(81)90324-6
https://doi.org/10.1016/0003-9861(81)90324-6
Publikováno v:
Biochemical Journal. 229:205-211
Experiments with carbamoyl phosphate synthetase (ammonia) in solution and in isolated mitochondria are reported which show the following. NH3 rather than NH4+ is the substrate of the enzyme. The apparent Km of NH3 for the purified enzyme is about 38
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8afee2c6458dfb4b0df1d358bc3cf1f8
https://doi.org/10.1042/bj2290205
https://doi.org/10.1042/bj2290205
Publikováno v:
Biochemical Journal. 257:251-257
Male mice carrying the spfash mutation have 5-10% of the normal activity of ornithine carbamoyltransferase, yet are only slightly hyperammonaemic and develop quite well. A study of liver mitochondria from normal and spfash males showed that they diff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2118275cba88b074a6ba305b2cac152c
https://doi.org/10.1042/bj2570251
https://doi.org/10.1042/bj2570251
Autor:
Mary Ellen Jones, Luisa Raijman
Publikováno v:
Archives of Biochemistry and Biophysics. 175:270-278
A procedure for the purification of rat liver carbamyl phosphate synthetase (ammonia) to homogeneity is described. The molecular weight of isolated active enzyme is 222,000 ± 10,000; that of the subunits obtained by denaturation with sodium dodecyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b32fe47095610bba64523a03e750213e
https://doi.org/10.1016/0003-9861(76)90508-7
https://doi.org/10.1016/0003-9861(76)90508-7
Publikováno v:
Biochimica et Biophysica Acta. 62:293-299
A procedure for the preparation of a very active carbamate kinase is presented. The reproducibility of the purification procedure and some of the kinetic parameters of the enzymatic reaction have been studied. The preparations are essentially homogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13e29a3e9de4859cb6c972f342a38bfd
https://doi.org/10.1016/0006-3002(62)90042-2
https://doi.org/10.1016/0006-3002(62)90042-2
Publikováno v:
Journal of Biological Chemistry. 235:2340-2342
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adbca840e7899dd61f20ece05e2b5278
https://doi.org/10.1016/s0021-9258(18)64623-x
https://doi.org/10.1016/s0021-9258(18)64623-x