scholarly journals A Vanadyl Sulfate-Bovine Serum Albumin Complex Stimulates the Release of Lipoprotein Lipase Activity from Isolated Rat Fat Pads through an Increase in the Cellular Content of cAMP and myo-Inositol 1,4,5-Trisphosphate.

1999 ◽  
Vol 22 (8) ◽  
pp. 780-786 ◽  
Author(s):  
Toshio MOTOYASHIKI ◽  
Mikoto MIYAKE ◽  
Aya YOSHIDA ◽  
Tetsuo MORITA ◽  
Hiroshi UEKI
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Bovine Serum ◽  
Vanadyl Sulfate ◽  
Lipoprotein Lipase Activity ◽  
Inositol 1,4,5 Trisphosphate ◽  
Fat Pads ◽  
Isolated Rat

Increasing effect of vanadate on lipoprotein lipase activity in isolated rat fat pads

1990 ◽  
Vol 279 (2) ◽  
pp. 291-297 ◽  
Author(s):  
Misaki Sera ◽  
Katsuhiro Tanaka ◽  
Tetsuo Morita ◽  
Hiroshi Ueki
Keyword(s):  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipoprotein Lipase Activity ◽  
Fat Pads ◽  
Isolated Rat

scholarly journals Increase in Lipoprotein Lipase Activity in Isolated Rat Adipose Tissue by Selenate.

1993 ◽  
Vol 16 (1) ◽  
pp. 6-10 ◽  
Author(s):  
Hiroshi UEKI ◽  
Yusuke OHKURA ◽  
Toshio MOTOYASHIKI ◽  
Nobuaki TOMINAGA ◽  
Tetsuo MORITA
Keyword(s):  
Adipose Tissue ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipoprotein Lipase Activity ◽  
Rat Adipose Tissue ◽  
Isolated Rat

scholarly journals The metabolism of L-tryptophan by isolated rat liver cells. Effect of albumin binding and amino acid competition on oxidatin of tryptophan by tryptophan 2,3-dioxygenase

1980 ◽  
Vol 186 (3) ◽  
pp. 977-986 ◽  
Author(s):  
S A Smith ◽  
C I Pogson
Keyword(s):  
Amino Acids ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Albumin Binding ◽  
Isolated Rat Liver ◽  
Free Tryptophan ◽  
Rat Liver Cells ◽  
Tryptophan Oxidation ◽  
Isolated Rat

1. Novel methods, using L-[ring-2-14C]tryptophan, are described for the measurement of tryptophan 2,3-dioxygenase activity and tryptophan accumulation in isolated rat liver cells. 2. The effects of bovine serum albumin, non-esterified fatty acids and neutral amino acids on tryptophan oxidation by hepatocytes and on the partition of tryptophan between free and albumin-bound forms were investigated. 3. Oxidation of physiological concentrations (0.1 mM) of tryptophan was inhibited by approx. 50% in the presence of 2% (w/v) bovine serum albumin; no effects were found at tryptophan concentrations of 0.5 mM and above. 4. Increases in free tryptophan concentrations produced by displacement of 0.1 mM-tryptophan from albumin-binding sites by palmitate resulted in increased flux through tryptophan dioxygenase. 5. Addition of a mixture of neutral amino acids, at plasma concentrations, to hepatocyte incubations had no effect on the rate of tryptophan oxidation. 6. It is concluded that alterations in free tryptophan concentrations consequent to changes in albumin binding may be an important factor in regulating tryptophan uptake and catabolism by the liver. The results are briefly discussed with reference to possible consequences on brain tryptophan metabolism.

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