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• W1989341321 abstract "1. Aspartate transcarbamoylase (carbamoyl phosphate:l-aspartate carbamoyl-transferase, EC 2.1.3.2) in hematopoietic mouse spleen can be fractionated into multiple forms. The activity in the soluble fraction can be separated into two fractions by chromatography on hydroxylapatite and are designated as Form I and II according to the order of elution from the column. Some activity sediments with the microsomal fraction (Form III). All these forms catalyze the formation of carbamoyl-aspartate from carbamoyl-P and aspartate. 2. When Form I was stored at 0° for 1 week and then rechromatographed on hydroxylapatite, some portion of activity behaved as Form II. The “conversion” is stimulated in the presence of dithiothreitol or mercaptoethanol. The physiological significance and the precise nature of the “conversion” are not yet known. 3. Upon centrifugation in a sucrose density gradient, Form I sediments at a S value of about 19, while Form II shows a broad distribution of S values, ranging from 22 to 45, with a peak at 35 S. 4. The three forms are not distinguished from each other by kinetic properties. All three forms have the same apparent Km values for aspartate (5.6 mM), and are inhibited by higher concentrations of aspartate, 20 mM or more. The Lineweaver-Burk plots for varying concentrations of carbamoyl-P are not linear, but concave downward, with all three forms. The apparent Km values obtained at lower concentrations of carbamoyl-P are smaller than those obtained at higher concentrations. 5. Inhibition by pyrimidine derivatives was examined at pH 9.2 and 7.6 for each of the three forms. Of eleven pyrimidine derivatives so far tested, only deoxythymidine and deoxyuridine at 4 mM inhibit the enzymic activity by about 15–30% at pH 9.2. Of the three forms, Form II is inhibited to a slightly greater extent than the others. At pH 7.6, the inhibition is more marked, and in addition to deoxythymidine and deoxyuridine, TTP and CTP at 4mM inhibit the enzyme activity by about 20–30%. In any case, the extent of inhibition is lower than 40%. 6. The function of aspartate transcarbamoylase regarding regulation of pyrimidine biosynthesis in mouse spleen as well as in other tissues is discussed." @default.
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• W1989341321 date "1970-12-01" @default.
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• W1989341321 title "Control of pyrimidine biosynthesis in mammalian tissues. III. Multiple forms of aspartate transcarbamoylase of mouse spleen" @default.
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• W1989341321 doi "https://doi.org/10.1016/0005-2744(70)90280-9" @default.
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