PREPARATION AND PROPERTIES OF TRANSKETOLASE FROM PORK LIVER
1960 ◽
Vol 38
(1)
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pp. 115-124
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Keyword(s):
Transketolase of pork liver has been purified 90-fold and separated from ribulose 5-phosphate 3-epimerase. The transketolase is most stable between pH 7.5 and 8.5 and below 40 °C. The pH range for optimum activity is between 7.6 and 8.1. Activation by magnesium ions or thiamine pyrophosphate could not be demonstrated, but thiamine pyrophosphate increased the stability of the enzyme. Sulphydryl agents, such as p-chloromercuriphenyl sulphonic acid and N-ethylmaleimide, and heavy metal ions, such as cupric, mercuric, and zinc, at relatively high concentrations inhibited the enzyme.
1960 ◽
Vol 38
(2)
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pp. 115-124
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Keyword(s):
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2000 ◽
Vol 73
(3)
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pp. 255-267
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2004 ◽
Vol 69
(7)
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pp. 541-547
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Keyword(s):
1987 ◽
Vol 35
(3)
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pp. 231-240
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Keyword(s):