Rapid partial purification of S-adenosyl-L-methionine decarboxylase by affinity chromatography

A Sepharose-ethylenediamine-PCMB column can be used to obtain a rapid purification of S-adenosyl-L-methionine decarboxylase. PCMB-affinity fractions from both rat liver and sea urchin eggs have high specific activity, particularly the latter. The activity of the purified rat liver enzyme is stimulat...

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Veröffentlicht in:	Life sciences (1973) 1974-05, Vol.14 (10), p.1907-1915
Hauptverfasser:	Manen, Carol-Ann, Russell, Diane H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Autoanalysis Binding Sites Carbon Radioisotopes Carboxy-Lyases - isolation & purification Chloromercuribenzoates Chromatography, Affinity Chromatography, Ion Exchange Cyanogen Bromide Electrophoresis Female Liver - enzymology Ovum - enzymology Polysaccharides Protein Binding Putrescine Rats S-Adenosylmethionine Sea Urchins Spectrophotometry, Ultraviolet Spermidine
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container_end_page	1915
container_issue	10
container_start_page	1907
container_title	Life sciences (1973)
container_volume	14
creator	Manen, Carol-Ann Russell, Diane H.
description	A Sepharose-ethylenediamine-PCMB column can be used to obtain a rapid purification of S-adenosyl-L-methionine decarboxylase. PCMB-affinity fractions from both rat liver and sea urchin eggs have high specific activity, particularly the latter. The activity of the purified rat liver enzyme is stimulated by the addition of either putrescine or spermidine, whereas the purified enzyme fraction from sea urchin eggs has no measurable activity without the addition of either putrescine or spermidine. In both preparations there is a stoichiometric relationship between the release of 14CO2 from S-adenosyl-L-carboxyl- 14C-methionine and the formation of spermidine.
doi_str_mv	10.1016/0024-3205(74)90407-X
format	Article
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PCMB-affinity fractions from both rat liver and sea urchin eggs have high specific activity, particularly the latter. The activity of the purified rat liver enzyme is stimulated by the addition of either putrescine or spermidine, whereas the purified enzyme fraction from sea urchin eggs has no measurable activity without the addition of either putrescine or spermidine. 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PCMB-affinity fractions from both rat liver and sea urchin eggs have high specific activity, particularly the latter. The activity of the purified rat liver enzyme is stimulated by the addition of either putrescine or spermidine, whereas the purified enzyme fraction from sea urchin eggs has no measurable activity without the addition of either putrescine or spermidine. In both preparations there is a stoichiometric relationship between the release of 14CO2 from S-adenosyl-L-carboxyl- 14C-methionine and the formation of spermidine.</abstract><cop>Netherlands</cop><pub>Elsevier Inc</pub><pmid>4847793</pmid><doi>10.1016/0024-3205(74)90407-X</doi><tpages>9</tpages></addata></record>
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subjects	Animals Autoanalysis Binding Sites Carbon Radioisotopes Carboxy-Lyases - isolation & purification Chloromercuribenzoates Chromatography, Affinity Chromatography, Ion Exchange Cyanogen Bromide Electrophoresis Female Liver - enzymology Ovum - enzymology Polysaccharides Protein Binding Putrescine Rats S-Adenosylmethionine Sea Urchins Spectrophotometry, Ultraviolet Spermidine
title	Rapid partial purification of S-adenosyl-L-methionine decarboxylase by affinity chromatography
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