1981
DOI: 10.1021/bi00507a045
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Multiple species of mammalian S-adenosylmethionine synthetase. Partial purification and characterization

Abstract: Two species of S-adenosylmethionine (S-Ado-Met) synthetase (EC 2.5.1.6) exist in rat liver cytosol and a distinct species of the enzyme exists in kidney cytosol. S-Ado-Met synthetases alpha and beta in rat liver cytosol have been partially purified about 200- and 80-fold, respectively. The apparent molecular weight estimated by gel filtration and the sedimentation coefficient are 210 000 and 9 S for S-Ado-Met synthetase alpha and 160 000 and 5.5 S for S-Ado Met synthetase beta. Both enzymes absolutely require … Show more

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Cited by 118 publications
(77 citation statements)
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“…The apparent Michaelis-Menten constants obtained by Lineweaver-Burk plots are reported in Table 2. The K , values calculated are in good agreement with those reported in the literature for mammalian CI and y forms [20,22,23] and human lymphocyte AdoMet synthetase [19]. Both double-reciprocal plots showed good linearity indicating the absence of cooperativity, in agreement with the data reported for the enzyme from E. coli [17], human lymphocytes [19] and erythrocytes [16].…”
Section: Michaelis Constants and Inhibition Studiessupporting
confidence: 89%
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“…The apparent Michaelis-Menten constants obtained by Lineweaver-Burk plots are reported in Table 2. The K , values calculated are in good agreement with those reported in the literature for mammalian CI and y forms [20,22,23] and human lymphocyte AdoMet synthetase [19]. Both double-reciprocal plots showed good linearity indicating the absence of cooperativity, in agreement with the data reported for the enzyme from E. coli [17], human lymphocytes [19] and erythrocytes [16].…”
Section: Michaelis Constants and Inhibition Studiessupporting
confidence: 89%
“…This finding implies that inorganic tripolyphosphate could be an enzyme-bound intermediate which is cleaved by a tripolyphosphatase intrinsically associated with AdoMet synthetase [12-141. AdoMet synthetase is distributed in both prokaryotic and eukaryotic organisms [5,15, 161 and it has been purified to homogeneity from Escherichiu coli [17] [20,23, 241. There is a general agreement that the y form is the major, if not the only form, in normal nonhepatic tissues of rat and man [20,23, 251.…”
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confidence: 99%
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