Zobrazeno 1 - 10
of 16
pro vyhledávání: '"R B, Frydman"'
Publikováno v:
The Journal of biological chemistry. 265(34)
[5,8-13C2]Spermidine was prepared by synthesis, and its binding to macromolecular structures of Escherichia coli was studied. When added to E. coli cells, the two signals of [13C]spermidine (C-5, 47.8 ppm, and C-8, 39.6 ppm; JC-C = 5.8 Hz) were stron
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1ec2fb98491f1fa8a4b020f227a89175
https://pubmed.ncbi.nlm.nih.gov/2249994
https://pubmed.ncbi.nlm.nih.gov/2249994
Biosynthesis of uroporphyrinogens. Interaction among 2-aminomethyltripyrranes and the enzymic system
Publikováno v:
Biochemistry. 17:115-120
Many hypotheses on uroporphyrinogen biosynthesis advanced the possibility that 2-aminomethyltripyrranes formed by porphobilinogen deaminase are further substrates or uroporphyrinogen III co-synthase in the presence of porphobilinogen. These proposals
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d0bf87bb2b69c439eee85a2409bcb74
https://doi.org/10.1021/bi00594a016
https://doi.org/10.1021/bi00594a016
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 954:114-125
The inhibitory effect of a series of 2-alkylputrescines on rat liver and Escherichia coli ornithine decarboxylase ( l -ornithine carboxy-lyase, EC 4.1.1.17) was examined. At 2.5 mM concentrations, 2-methyl-, 2-propyl-, 2-butyl-, 2-pentyl- and 2-hexyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64d9c273bb305faa75e38c4ff7cdbe08
https://doi.org/10.1016/0167-4838(88)90061-1
https://doi.org/10.1016/0167-4838(88)90061-1
Publikováno v:
Chemischer Informationsdienst. 9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::33124597860839b60aa92e210a1a3995
https://doi.org/10.1002/chin.197801353
https://doi.org/10.1002/chin.197801353
Publikováno v:
The Journal of biological chemistry. 262(31)
Porphobilinogen oxygenase oxidizes porphobilinogen to 2-hydroxy-5-oxo-porphobilinogen. This enzyme isolated from wheat germ has been purified to homogeneity, as judged by polyacrylamide gel electrophoresis under both nondenaturing and denaturing cond
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d9c2f3102953978f17566e3c8f8f3cf2
https://pubmed.ncbi.nlm.nih.gov/2822713
https://pubmed.ncbi.nlm.nih.gov/2822713
Autor:
R B, Frydman, G, Feinstein
Publikováno v:
Biochimica et biophysica acta. 350(2)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::da3bf784fdeea8c26ac617618fc351f9
https://pubmed.ncbi.nlm.nih.gov/4847568
https://pubmed.ncbi.nlm.nih.gov/4847568
Publikováno v:
Biochimica et biophysica acta. 704(2)
The enzymatic oxidations of [alpha-14C]deuterohemin IX, [alpha-14C]hematohemin IX and 2,4-diacetyl[alpha-14C]deuterohemin IX were carried out by using a microsomal heme oxygenase system from rat liver in combination with the biliverdin reductase from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::06a622f4376641abdff1f18f10b13222
https://pubmed.ncbi.nlm.nih.gov/6896662
https://pubmed.ncbi.nlm.nih.gov/6896662
Publikováno v:
Chemischer Informationsdienst. 10
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77e0274b72a9f741c12d625652188f1d
https://doi.org/10.1002/chin.197934210
https://doi.org/10.1002/chin.197934210
Publikováno v:
Biochimica et biophysica acta. 787(2)
The substrate specificity of the different molecular forms of biliverdin reductase (bilirubin:NAD(P)+ oxidoreductase, EC 1.3.1.24) using biliverdin XIII alpha, XIII beta and XIII gamma was examined. It was found that molecular form 1 (the major form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::15250b0fdd31ff65077bbb4d64000143
https://pubmed.ncbi.nlm.nih.gov/6733114
https://pubmed.ncbi.nlm.nih.gov/6733114