Human erythrocyte AMP: Pyrophosphate phosphoribosyltransferase (EC 2.4.2.7)
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چکیده
منابع مشابه
Baker ’ s Yeast UMP : Pyrophosphate Phosphoribosyltransferase
Baker’s yeast UMP:pyrophosphate phosphoribosyltransferase (EC 2.4.2.9) has been extensively purified and the final preparation seemed to be pure but not homogeneous. The native enzyme showed a molecular weight of 80,000 calculated by gel filtration; disc gel electrophoresis performed in the presence of sodium dodecyl sulfate and reducing agents showed two dissimilar subunits and the sum of thei...
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The binding of purified human erythrocyte AMP deaminase to human erythrocyte membranes and the effect of binding on enzyme catalytic activity was investigated. AMP deaminase binds preferentially and specifically to the cytoplasmic surface of the erythrocyte membrane. The binding is saturable, reversible, and responsive to alterations of pH, of ionic strength, and of ATP and AMP concentrations. ...
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IMP:pyrophosphate phosphoribosyltransferase (IPPase) (EC 2.4.2.8) has been purified over 7000-fold from human erythrocytes. The purified enzyme moved as a single band on disc electrophoresis. Antisera prepared in rabbits and rats against the purified enzyme precipitated and neutralized the enzyme, but had no effect on AMP-pyrophosphate phosphoribosyltransferase (EC 2.4.2.7) activity. Evidence w...
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Hypoxanthine phosphoribosyltransferase (inosine monophosphate: pyrophosphate phosphoribosyltransferase EC 2.4.2.8) has been purified SO-fold from an acid-treated lysate of human erythrocytes. The average particle weight of the enzyme was estimated by gel filtration at 60,000. Between the pH values of 7.1 and 9.1 no marked difference in the initial velocity of IMP synthesis was observed. Kinetic...
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Human adenine phosphoribosyltransferase has been purified 33,000-fold from erythrocytes to a specific activity of 9.58 pmoles of AMP formed per mg of protein per min. The native enzyme has a molecular weight of 34,000 and is composed of three subunits of equal molecular weight which appear to be associated by noncovalent forces. The highly purified enzyme is maximally active over a broad pH ran...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1968
ISSN: 0014-5793
DOI: 10.1016/0014-5793(68)80054-7