Lipids Part C by John M. Lowenstein (Eds.)

By John M. Lowenstein (Eds.)

The significantly acclaimed laboratory usual, Methods in Enzymology, is among the such a lot hugely revered guides within the box of biochemistry. considering that 1955, each one quantity has been eagerly awaited, usually consulted, and praised by means of researchers and reviewers alike. The sequence includes a lot fabric nonetheless correct this present day - really a vital book for researchers in all fields of lifestyles sciences

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Dickstein, and F. Ahmad, Fed. Proc. 37, 1403 (1978). 18 This biotin content corresponds to 1 mol of biotin per 240,000 g of carboxylase protein. The biotin content of rat mammary gland carboxylase is equivalent to that reported for rat liver a'19 and bovine adipose tissue ° enzymes. 5 nmol of phosphate. y 6 mol of phosphate are present per 240,000 g of protein. The phosphate content is based upon protein determined by the method of Bradford, zl using ovalbumin as standard. 3 mol of phosphate per 240,000 g of protein.

Inoue and J. M. Lowenstein, J. Biol. Chem. 247, 4825 (1972). 2 Acetyl-CoA: carbon-dioxide ligase (ADP-forming) By D. GRAHAME H A R D I E , PAUL S. GuY, and PHILIP COHEN Acetyl-CoA carboxylase Acetyl-CoA + CO2 + ATP-~ malonyl-CoA + ADP + Pi Fatty acid synthase Acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H ÷ --~ palmitic acid + 8 CoA + 7 CO2 + 6 H20 + 14 NADP ÷ METHODS IN ENZYMOLOGY, VOL. 7l Copyright © 198! by Academic Press, Inc. All rights of reproduction in any form reserved. ISBN 0-12-181971-X [3] A C E T Y L - C o A CARBOXYLASE AND FATTY ACID SYNTHASE 27 The purification of acetyl-CoA carboxylase and fatty acid synthase from a number of different sources has been described in previous volumes (XIV, XXXV).

0. It is not yet clear why the polyethylene glycol preparations have such low specific enzymatic activities. Attempts to activate these preparations have been unsuccessful thus far. TM Activators and Inhibitors. The crude and the pure enzyme is activated by citrate. As stated previously the crude, but not the purified, enzyme requires preincubation with citrate prior to assay. The purified enzyme shows almost complete dependence upon citrate for activity. Maximal activation occurs in the presence of 25-30 mM citrate with 30 mM magnesium acetate present.

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