Zobrazeno 1 - 10
of 72
pro vyhledávání: '"Charles M. Baugh"'
The pteridines in their multitude of forms fulfill many roles in nature ranging from pigments to cofactors for numerous redox and one-carbon transfer reactions. This extraordinary diversity of function is unified by the unique chemistry of the pterid
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461362876
Chemistry and Biology of Pteridines and Folates
Chemistry and Biology of Pteridines and Folates
The proceedings of the Tenth International Symposium on [title], held in Orange Beach, Alabama, March 1993, provide new insights into folate enzymology, tetrahydrobiopterin and molybdopterin biosynthesis and function, enzyme synthesis and regulation,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f45ec8683b0ba2e9e621b7da842ffcf
https://doi.org/10.1007/978-1-4615-2960-6
https://doi.org/10.1007/978-1-4615-2960-6
Publikováno v:
Analytical Biochemistry. 146:52-58
Tritium-labeled [6 S ]-tetrahydropteroylpolyglutamates of high radiospecific activity were prepared from the corresponding pteroylpolyglutamates. Malic enzyme and d,l -[2- 3 H]malate were used as a generating system to produce [4A- 3 H]NADPH which wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78107356e8d49b8ae2b2ada4c6bbb83a
https://doi.org/10.1016/0003-2697(85)90394-x
https://doi.org/10.1016/0003-2697(85)90394-x
Autor:
Rowena G. Matthews, Charles M. Baugh
Publikováno v:
Biochemistry. 19:2040-2045
Dihydrofolate and dihydropteroylpolyglutamates inhibit pig liver methylenetetrahydrofolate reductase. In all cases the inhibition is linearly competitive with respect to methylenetetrahydrofolate. The Ki values decrease with each additional glutamyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63bff799f626e2296388f03d65069207
https://doi.org/10.1021/bi00551a005
https://doi.org/10.1021/bi00551a005
Publikováno v:
Gastroenterology. 68:261-269
The technique of human jejunal perfusion was used to study the process of digestion and absorption of conjugated folates in five healthy volunteers. The test solution of isotonic saline contained equimolar concentrations of purified [3H]pteroylmonogl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e3d1509492fb19b2b22dc2461a18173
https://doi.org/10.1016/s0016-5085(75)80007-2
https://doi.org/10.1016/s0016-5085(75)80007-2
Publikováno v:
Biochemical and Biophysical Research Communications. 71:527-534
In contrast to (+)5,10-methylenetetrahydropteroylmonoglutamate which does not bind to Lactobacillus casei thymidylate synthetase, the corresponding tetraglutamate analog binds to a single site with a KD = 2 × 10−5 M. Alkylation of one of the enzym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::702bb62056b341c9289d68bb15dbe719
https://doi.org/10.1016/0006-291x(76)90819-6
https://doi.org/10.1016/0006-291x(76)90819-6
Publikováno v:
Analytical Biochemistry. 115:163-169
Tissue folate polyglutamate chain lengths have been estimated by incorporation of the 5,10-methylenetetrahydrofolate polyglutamate form of the cofactor into ternary complexes with Lactobacillus casei thymidylate synthetase and [3H]fluorodeoxyuridylat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1319c92b3529f96df5d96393ee44043
https://doi.org/10.1016/0003-2697(81)90540-6
https://doi.org/10.1016/0003-2697(81)90540-6
Publikováno v:
Biochemistry. 13:4952-4957
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1785be0f8e1a254c07b34775c0108ec
https://doi.org/10.1021/bi00721a012
https://doi.org/10.1021/bi00721a012
Publikováno v:
Journal of Medicinal Chemistry. 21:673-677
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a05b3d403c8929fa1726157dd4b7233
https://doi.org/10.1021/jm00205a015
https://doi.org/10.1021/jm00205a015
Publikováno v:
Journal of Biological Chemistry. 249:4100-4103
(l)-Tetrahydropteroyltriglutamate and (l)-tetrahydropteroylhexaglutamate were prepared and tested as substrates for thymidylate synthetase (EC 2.1.1.6) (methylenetetrahydrofolate:deoxyuridylate C-methyltransferase) from Lactobacillus casei. Both tetr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7650439ea37cc00cb7bc3ca98e305c76
https://doi.org/10.1016/s0021-9258(19)42488-5
https://doi.org/10.1016/s0021-9258(19)42488-5