Effects of coenzyme A and pH on the reactions catalysed by lactating bovine mammary-gland fatty acid synthase

1981 ◽  
Vol 9 (6) ◽  
pp. 556-557 ◽  
Author(s):  
PETER F. DODDS ◽  
SOMA KUMAR
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Coenzyme A ◽  
Bovine Mammary Gland

Active site directed inactivation of rat mammary gland fatty acid synthase by 3-chloropropionyl coenzyme A

Biochemistry ◽  
1986 ◽  
Vol 25 (2) ◽  
pp. 468-473 ◽  
Author(s):  
Henry M. Miziorko ◽  
Christine E. Behnke ◽  
Patricia M. Ahmad ◽  
Fazal Ahmad
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Active Site ◽  
Fatty Acid Synthase ◽  
Coenzyme A ◽  
Rat Mammary Gland

scholarly journals Regulation of lipogenic capacity in lactating rats

1982 ◽  
Vol 208 (3) ◽  
pp. 611-618 ◽  
Author(s):  
M R Grigor ◽  
A Geursen ◽  
M J Sneyd ◽  
S M Warren
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Malic Enzyme ◽  
Fatty Acid Synthase ◽  
Specific Activity ◽  
Mammary Glands ◽  
Lipogenic Enzymes ◽  
Pregnancy And Lactation ◽  
Specific Activities

1. The rate of mammary-gland lipogenesis measured in vivo from 3H2O was suppressed after decreasing the milk demand by decreasing the number of pups from ten to two or three, as well as by giving diets containing lipid [Grigor & Warren (1980) Biochem. J. 188, 61-65]. 2. The specific activities of the lipogenic enzymes fatty acid synthase, glucose 6-phosphate dehydrogenase and ‘malic’ enzyme increased between 6- and 10-fold in the mammary gland and between 2- and 3-fold in the livers during the first 10 days of lactation. The increases in specific activity coupled with the doubling of liver mass which occurred during pregnancy and lactation resulted in considerable differences in total liver activities when compared with virgin animals. 3. Although consumption of a diet containing 20% peanut oil suppressed the activities of the three lipogenic enzymes in the livers, only the ‘malic’ enzyme was affected in the mammary glands. 4. In contrast, decreased milk demand did not affect the specific activities of any of the liver enzymes, whereas it resulted in suppression of all three lipogenic enzymes of the mammary glands. There was no effect on either the cytoplasmic malate dehydrogenase or the lactate dehydrogenase of the mammary gland. 5. In all the experiments performed, the activity of the fatty acid synthase correlated with the amount of material precipitated by the rabbit antibody raised against rat fatty acid synthase.

scholarly journals Rat mammary-gland fatty acid synthase. A simple purification procedure and stoicheiometry of CoA ester binding

1982 ◽  
Vol 203 (1) ◽  
pp. 45-50 ◽  
Author(s):  
P M Ahmad ◽  
D S Feltman ◽  
F Ahmad
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Specific Activity ◽  
Simple Procedure ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Performic Acid ◽  
Mammary Tissue ◽  
Rat Mammary Gland

A simple procedure was devised which allows purification of rat lactating-mammary-gland fatty acid synthase to a high degree of purity, with recoveries of activity exceeding 50%. Over 50 mg of enzyme was isolated from 60 g of mammary tissue. The specific activity of the purified enzyme was about 2.5 mumol of NADPH oxidized/min per mg of protein at 37 degrees. The enzyme appeared homogeneous by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and by immunodiffusion analysis. Each mol (Mr 480 000) of the enzyme bound 3 mol of acetyl and 3-4 mol of malonyl groups when the binding experiments were performed at 0 degrees for 30 s. The presence of NADPH did not influence the binding stoicheiometry for these acyl-CoA derivatives. Approx. 2 mol of taurine was found per mol of the performic acid-oxidized enzyme, suggesting that there were 2 mol of 4′-phosphopantetheine in the native enzyme. Rat mammary-gland fatty acid synthase required free CoA for activity.

scholarly journals Protein degradation during terminal cytodifferentiation. Studies on mammary gland in organ culture

1980 ◽  
Vol 192 (1) ◽  
pp. 311-320 ◽  
Author(s):  
C J Wilde ◽  
N Paskin ◽  
J Saxton ◽  
R J Mayer
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Protein Degradation ◽  
Degradation Rate ◽  
Fatty Acid Synthase ◽  
Average Rate ◽  
Cytosol Fraction ◽  
Isotope Method ◽  
Degradation Rates ◽  
Double Isotope

1. In mammary gland explants subjected to experimental manipulation, average rates (during 24 h periods) of degradation of fatty acid synthase, casein and cytosol-fraction proteins were measured by a double-isotope method. Rates of degradation of fatty acid synthase were also computed from measurements of changing enzyme amount and rate of synthesis. 2. During the period of most rapid enzyme accumulation there is a transient decrease in the computed rate of degradation of fatty acid synthase. Removal of hormones produces a rapid increase in the computed rate of degradation of the enzyme. 3. The average rate of degradation of fatty acid synthase measured by the double-isotope method is low in the presence of hormones, and increases on hormone removal. This increase in degradation rate is inhibited by adrenaline and further blocked by insulin. NH4Cl (10 mM) also partially inhibits the increase in protein degradation on hormone removal. 4. The pattern of changes in the average rate of degradation of cytosol-fraction proteins is similar to that for fatty acid synthase alone. There is no relationship between subunit molecular weight and rate of degradation under all experimental conditions. 5. Isotope ratios for resolved cytosol protein mixtures are transformed logarithmically to make the standard deviations an estimate of heterogeneity of degradation rates. By this analysis, in some conditions there appears to be significant measureable heterogeneity of degradation rates. 6. Little degradation of casein is measured in the presence of hormones, but a marked increase in the rate of degradation can be measured when hormones are removed. Whereas at 24-48h NH4Cl (10 mM) has little effect on this enhanced rate of degradation, at 48-72h it causes a large decrease in degradation rate. 7. Results are discussed in terms of a two-component degradation system in mammary gland explants.

Association of cytosolic lipids with fatty acid synthase from lactating mammary gland

1993 ◽  
Vol 25 (4) ◽  
pp. 533-543 ◽  
Author(s):  
Brigitte H. Keon ◽  
Debabrota Ghosal ◽  
Thomas W. Keenan
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Lactating Mammary Gland
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