. Cell chemistry; a collection of papers dedicated to Otto Warburg on the occasion of his 70th birthday. Warburg, Otto Heinrich, 1883-; Biochemistry. A. 270 280 340 290 300 310 320 WAVE LENGTH {m/<) Fig. 5. Spectral changes accompanying the enzy- matic synthesis and breakdown of S-acetoacetyl CoA at pH Volume, ml; d = cm; temp. 25°.—O—O—S-SuccinylCoA('^^ fiM). — 0 — %— After establishment of equilibrium on addition of acetoacetate (50 fiM) and trans- ferase (60 jug of protein). —/\—/\— After further addition of CoA-SH ( fiM) and thiolase (90 /ig of protein). Acetoacetate
. Cell chemistry; a collection of papers dedicated to Otto Warburg on the occasion of his 70th birthday. Warburg, Otto Heinrich, 1883-; Biochemistry. A. 270 280 340 290 300 310 320 WAVE LENGTH {m/<) Fig. 5. Spectral changes accompanying the enzy- matic synthesis and breakdown of S-acetoacetyl CoA at pH Volume, ml; d = cm; temp. 25°.—O—O—S-SuccinylCoA('^^ fiM). — 0 — %— After establishment of equilibrium on addition of acetoacetate (50 fiM) and trans- ferase (60 jug of protein). —/\—/\— After further addition of CoA-SH ( fiM) and thiolase (90 /ig of protein). Acetoacetate and CoA-SH added to both blank and experimental cells. MgClg ( /.iM) present in reaction mixture. »- SUCCINATE i. 12 16 MINUTES Fig. 6. Optical demonstration of transferase and thiolase activities. Volume, ml; d — cm; pH, ; temp, 25°. Upper curve: Transferase (17 fig of protein) added at zero time to a mix- ture of succinyl CoA {r~^ /liM) and acetoace- tate (50 fiM); succinate (40 /nM) added at the arrow. Lower curve: Transferase (17 //g of protein) added at zero time to a mixture of succinyl CoA {'-^ fiM) and acetoacetate (50 /nM); CoA-SH ( /uM) and thiolase ( fig of protein) added at the arrow. Other details as in Fig. 5. reaction as followed at 305 m/x are shown in Fig. 6. The upper curve shows the increase in absorption at 305 m/x on adding transferase to a mixture of succinyl CoA and aceto- acetate and the reversal of the reaction by succinate after equilibrium was established. The equilibrium constant of the transferase reaction (/v^^ = (Succinate) (acetoacetyl-S- CoA)/Succinyl-S-CoA) (acetoacetate)) is about lO^^ at pH The acetoacetyl CoA formed by the reaction between succinyl CoA and aceto- acetate, in the presence of transferase, was isolated as a crude alcohol-insoluble barium salt and further purified by paper chromatography^^. In ethanol-acetate its Rp is at 24°, while that of acetoacetate is L
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