Zobrazeno 1 - 10
of 111
pro vyhledávání: '"M. Kutáček"'
Autor:
Esther Simón, H. Gautier, Ella M. Kof, P. K. Malec, M. M. Altamura, Josef Eder, Luisa Moysset, T. K. Kashina, G. Giuliano, S. Obrenovic, L. Michalczuk, E. Sandu, V. Čermák, A. Mann, G. V. Shishcanu, P. J. Lumsden, M. Zivkovic, W. T. Griffiths, Esther Llambrich, N. Lebedev, R. B. Malina, B. Borkowska, V. I. Kefeli, J. A. Youngs, C. Varlet-Grancher, R. A. Rinaldi, F. M. Maas, M. F. Danilova, M. Tomassi, M. Kutáček
Publikováno v:
Biologia plantarum. 36:S59-S65
Autor:
J. Rovenská, M. Kutáček
Publikováno v:
Plant Growth Regulation. 10:313-327
Problems of IAA biosynthesis, IAA precursors and IAA biosynthetic pathways in Agrobacterium tumefaciens-transformed plant tissue, especially in tobacco tissue culture are reviewed. The knowkedge about levels of IAA and the IAA biosynthetic pathways i
Publikováno v:
Biologia plantarum. 33:277-286
The transaminations of L-tryptophan (L-trp) and of L-phenylalanine (L-phe) are catalysedin vitro by the same non-specific aminotransferase. The transaminations procceed at the same pH (pH 8.5) and temperature (45 °C) optima, have parallel increases
Publikováno v:
Biologia plantarum. 33
In pea, maize and tomato plants a hitherto undescribed L-tryptophan dehydrogenase activity (TDH) has been detected. This enzyme catalyzes the reversible formation of indolepyruvic acid (IPyA) from L-tryptophan (L-trp). TDH and L-glutamate dehydrogena
Publikováno v:
Biologia plantarum. 33
Indole-3-acetaldehyde oxidase (IAAld-oxidase) occurs in pea in two forms, of which the first, more active enzyme, has its pH optimum at 4.5, while the second, barely half as active, has a pH optimum at 7.0. Only the pH 4.5 oxidase can be resolved fro
Publikováno v:
Biologia Plantarum. 23:220-227
In the seeds ofAllium altaicun (Pall.)Reyse a set of enzymes was found, metabolizing choline esters, composed of active choline esterases and choline acetyltransferase. Choline esterase cleaving acetylcholine occurs in five isoenzymes. The enzyme pre
Publikováno v:
Theoretical and Applied Genetics. 46:19-23
The activity of glutamate-oxalacetate and glutamate-pyruvate transaminases (GOT 2.6.1.1., GPT 2.6.1.2.) was determined in seedlings of normal and opaque-2 maize. The activity of these transaminases was determined in homozygotes +/+ and o2/o2, their F
Autor:
M. M. Ebeid, M. Kutáček
Publikováno v:
Biologia Plantarum. 21:170-177
The effect of manganese chloride (10 mg Mn l-1), EDTA (18 mg l-1) and a mixture of these compounds on the nitrogen balance in maize xylem exudate was investigated. The compounds were applied as experimental solutions to the roots of 20 day old plants
Autor:
M. Kutáček, Eva Zažímalová
Publikováno v:
Plant Growth Regulation. 3:15-26
A binding site for auxins was found in the 50,000g pellet from a homogenate of shoots from dark-grown wheat seedlings. The optimum conditions for the binding of native auxin, IAA, were within the range of physiological conditions of growth (pH 5.2, t
Publikováno v:
Biologia Plantarum. 23:345-350
The increased activity of GOT (E.C.2.6.1.1.) and GPT (E.C.2.6.1.2.) transaminases in maize seedlings found as a marker of genotype opaque-2, was investigated in extirped sprouts of both genotypes, normal and opaque-2. The enzymatic activity was deter