Zobrazeno 1 - 10
of 145
pro vyhledávání: '"R.M. Khomutov"'
Autor:
T. Hyvonen, Terho O. Eloranta, R.M. Khomutov, A.R. Khomutov, Tuomo A. Keinänen, Jouko Vepsäläinen, Risto A. Kauppinen
Publikováno v:
Analytical Biochemistry. 208:35-43
A radiometric determination of monoaminooxy analogues of naturally occurring polyamines is described in which [2-14C]acetone is employed as reagent. The reagent is volatile while the oxime product is not allowing unreacted reagent to be removed and t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47ac79047f531bd50553aac151a39730
https://doi.org/10.1006/abio.1993.1005
https://doi.org/10.1006/abio.1993.1005
Publikováno v:
Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0c51587ef04ccdfc91f0ded8bcd24439
https://doi.org/10.1016/b978-0-08-040820-0.50117-5
https://doi.org/10.1016/b978-0-08-040820-0.50117-5
Publikováno v:
Scopus-Elsevier
The effects on cultured baby hamster kidney cells of 1-aminooxy-3-aminopropane, a potent new inhibitor of mammalian ornithine and S-adenosylmethionine decarboxylases and of spermidine synthase, were studied. At 0.5 mM concentration in the culture med
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8ab90d27fd2f3117f64a9d0f4ad0141
https://doi.org/10.1016/s0021-9258(18)37933-x
https://doi.org/10.1016/s0021-9258(18)37933-x
Publikováno v:
Biochemical and Biophysical Research Communications. 35:318-323
The conversion of substrate into product catalyzed by an enzyme with a prosthetic group is known to involve a number of stages during which the substrate is bound covalently with the coenzyme. For pyridoxal enzymes, and particularly for transaminases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49161ec38b1ef3efafa6e43bbb7d74bc
https://doi.org/10.1016/0006-291x(69)90501-4
https://doi.org/10.1016/0006-291x(69)90501-4
Publikováno v:
FEBS Letters. 130:85-87
The formation of peptide bonds catalyzed by ribosomes has been studied using a number of 2’(3’)-Opeptidyladenosine-5’-phosphates or analogs of tRNA [ 11. The present work describes the peptide donor properties of the organophosphorus analog pA(
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5637ac4df5eb4e3e60a4bae9338bf335
https://doi.org/10.1016/0014-5793(81)80671-0
https://doi.org/10.1016/0014-5793(81)80671-0
Publikováno v:
FEBS Letters. 91:246-248
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9bd6eb9fb911afc0b50538c9b24aed7
https://doi.org/10.1016/0014-5793(78)81183-1
https://doi.org/10.1016/0014-5793(78)81183-1
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 171:369-371
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ec1e3886c377d5f7dba005eaf094ee9
https://doi.org/10.1016/0005-2744(69)90174-0
https://doi.org/10.1016/0005-2744(69)90174-0
Publikováno v:
FEBS Letters. (1-2):208-210
Well-known aminoacyl-tRNA synthetase (ARSase) inhibitors, namely the analogues of amino acids and aminoacyl adenylates (aminoalkyl- and aminophosphonyl adenylates with K i ⋍ 0.1 μM) as well as the diadenosine 5',5'''- p 1 , p 4 -tetraphosphate (Ap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d133e5be252411cf970bf00c25dd3df8
Akademický článek
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Autor:
L. Kauppinen, T. Paalanen, Terho O. Eloranta, R.M. Khomutov, Raija-Leena Pajula, Lars Paulin, Leif C. Andersson, Tapani Hyvönen, Hannu Pösö, Eija Karvonen
Publikováno v:
Biochemical and biophysical research communications. 130(2)
1-Aminooxy-3-aminopropane was shown to be a potent competitive inhibitor (Ki = 3.2 nM) of homogenous mouse kidney ornithine decarboxylase, a potent irreversible inhibitor (Ki = 50 μM) of homogeneous liver adenosylmethionine decarboxylase and a poten
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1a5302fa25173360c4e769edc07ca0d
https://pubmed.ncbi.nlm.nih.gov/3861182
https://pubmed.ncbi.nlm.nih.gov/3861182