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

Kyoung Hee Nam, Sun Hi Lee, JooHun Lee

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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 non-denaturing PAGE. The purified ADC has an M(r) of 240 kDa based on gel filtration chromatography and is a trimer of identical subunits which has an estimated M(r) of 74 kDa based on SDS-PAGE. ADC is active between 30 and 50°C and has a K(m) value of 46.1 μM. ADC is very sensitive to agmatine or putrescine but not to spermidine or spermine. In the presence of 0.5 mM agmatine (or putrescine), the enzyme activity was inhibited by 70%. However, at the same concentration of spermidine (or spermine), the enzyme activity was inhibited by only 10-20%.

Original languageEnglish
Pages (from-to)1150-1155
Number of pages6
JournalPlant and Cell Physiology
Volume38
Issue number10
DOIs
Publication statusPublished - 1997 Jan 1

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Agmatine
agmatine
arginine decarboxylase
Hypocotyl
Putrescine
Spermidine
Spermine
spermine
spermidine
putrescine
Soybeans
hypocotyls
Gel Chromatography
Glycine max
enzyme activity
soybeans
Native Polyacrylamide Gel Electrophoresis
Ammonium Sulfate
Enzymes
affinity chromatography

All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science
  • Cell Biology

Cite this

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abstract = "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 non-denaturing PAGE. The purified ADC has an M(r) of 240 kDa based on gel filtration chromatography and is a trimer of identical subunits which has an estimated M(r) of 74 kDa based on SDS-PAGE. ADC is active between 30 and 50°C and has a K(m) value of 46.1 μM. ADC is very sensitive to agmatine or putrescine but not to spermidine or spermine. In the presence of 0.5 mM agmatine (or putrescine), the enzyme activity was inhibited by 70{\%}. However, at the same concentration of spermidine (or spermine), the enzyme activity was inhibited by only 10-20{\%}.",
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Purification and characterization of arginine decarboxylase from soybean (Glycine max) hypocotyls. / Nam, Kyoung Hee; Lee, Sun Hi; Lee, JooHun.

In: Plant and Cell Physiology, Vol. 38, No. 10, 01.01.1997, p. 1150-1155.

Research output: Contribution to journalArticle

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AB - 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 non-denaturing PAGE. The purified ADC has an M(r) of 240 kDa based on gel filtration chromatography and is a trimer of identical subunits which has an estimated M(r) of 74 kDa based on SDS-PAGE. ADC is active between 30 and 50°C and has a K(m) value of 46.1 μM. ADC is very sensitive to agmatine or putrescine but not to spermidine or spermine. In the presence of 0.5 mM agmatine (or putrescine), the enzyme activity was inhibited by 70%. However, at the same concentration of spermidine (or spermine), the enzyme activity was inhibited by only 10-20%.

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