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agmatine/soya

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Purification of monomeric agmatine iminohydrolase from soybean.

Watumiaji waliosajiliwa tu ndio wanaweza kutafsiri nakala
Ingia / Ingia
Agmatine iminohydrolase (EC 3.5.3.12) was purified to homogeneity from the cytosol of soybean (Glycine max) axes by chromatographic separations on Sephadex G-25, Bio-rex 70, and agmatine-affinity columns. The enzyme was homogeneous by the criteria of analytical gel electrophoresis. Molecular weights

Purification and characterization of arginine decarboxylase from soybean (Glycine max) hypocotyls.

Watumiaji waliosajiliwa tu ndio wanaweza kutafsiri nakala
Ingia / Ingia
Arginine decarboxylase (EC 4.1.1.19) was purified from soybean, Glycine max, hypocotyls by a procedure which includes ammonium sulfate fractionation, acetone precipitation, gel filtration chromatography, and affinity chromatography. Using this procedure, ADC was purified to one band in

Influence of cultivar and germination on bioactive amines in soybeans (Glycine max L. Merril).

Watumiaji waliosajiliwa tu ndio wanaweza kutafsiri nakala
Ingia / Ingia
The levels of amines in soybeans as affected by cultivar in two consecutive years and by germination were investigated. Spermidine, spermine, putrescine, agmatine, and cadaverine were detected, whereas tyramine, histamine, tryptamine, serotonine, and phenylethylamine were not. Spermidine was the

Purification of S-adenosylmethionine decarboxylase from soybean.

Watumiaji waliosajiliwa tu ndio wanaweza kutafsiri nakala
Ingia / Ingia
S-Adenosylmethionine decarboxylase (EC 4.1.1.19) was purified to homogeneity from the cytosol of soybean (Glycine max) axes by ammonium sulfate fractionation, DEAE-Sepharose and methylglyoxalbis(guanylhydrazone)-Sepharose 6B chromatographies. The enzyme was free from diamine oxidase activity. The

A new S-adenosylmethionine decarboxylase from soybean axes.

Watumiaji waliosajiliwa tu ndio wanaweza kutafsiri nakala
Ingia / Ingia
A new active S-adenosylmethionine decarboxylase (EC 4.1.1.50) (SAMDC II) was extracted from soybean (Glycine max) axes. The enzyme was purified to homogeneity by ammonium sulfate fractionation, DEAE-Sepharose and methylglyoxalbis(guanylhydrazone) (MGBG)-Sepharose 6B chromatographies. The molecular
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