Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis. / Rasmussen, J T; Faergeman, N J; Kristiansen, K; Knudsen, J.

In: Biochemical Journal, Vol. 299 ( Pt 1), 1994, p. 165-70.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Rasmussen, JT, Faergeman, NJ, Kristiansen, K & Knudsen, J 1994, 'Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis', Biochemical Journal, vol. 299 ( Pt 1), pp. 165-70. <http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1138036>

APA

Rasmussen, J. T., Faergeman, N. J., Kristiansen, K., & Knudsen, J. (1994). Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis. Biochemical Journal, 299 ( Pt 1), 165-70. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1138036

Vancouver

Rasmussen JT, Faergeman NJ, Kristiansen K, Knudsen J. Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis. Biochemical Journal. 1994;299 ( Pt 1):165-70.

Author

Rasmussen, J T ; Faergeman, N J ; Kristiansen, K ; Knudsen, J. / Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis. In: Biochemical Journal. 1994 ; Vol. 299 ( Pt 1). pp. 165-70.

Bibtex

@article{95f1f2700f0811de8478000ea68e967b,
title = "Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis",
abstract = "The dissociation constants for octanoyl-CoA, dodecanoyl-CoA and hexadecanoyl-CoA binding to acyl-CoA-binding protein (ACBP) were determined by using titration microcalorimetry. The KD values obtained, (0.24 +/- 0.02) x 10(-6) M, (0.65 +/- 0.2) x 10(-8) M and (0.45 +/- 0.2) x 10(-13) M respectively, were much lower than expected. ACBP was able to extract hexadecanoyl-CoA from phosphatidylcholine membranes immobilized on a nitrocellulose membrane. The acyl-CoA/ACBP complex formed was able to transport acyl-CoA to mitochondria or microsomes in suspension, or to microsomes immobilized on a nitrocellulose membrane, and to donate them to beta-oxidation or glycerolipid synthesis in mitochondria or microsomes, respectively.",
author = "Rasmussen, {J T} and Faergeman, {N J} and K Kristiansen and J Knudsen",
note = "Keywords: Acyl Coenzyme A; Animals; Biological Transport; Calorimetry; Carrier Proteins; Cattle; Diazepam Binding Inhibitor; Female; Glycerides; Intracellular Membranes; Male; Microsomes; Mitochondria; Oxidation-Reduction; Rabbits; Rats",
year = "1994",
language = "English",
volume = "299 ( Pt 1)",
pages = "165--70",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",

}

RIS

TY - JOUR

T1 - Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis

AU - Rasmussen, J T

AU - Faergeman, N J

AU - Kristiansen, K

AU - Knudsen, J

N1 - Keywords: Acyl Coenzyme A; Animals; Biological Transport; Calorimetry; Carrier Proteins; Cattle; Diazepam Binding Inhibitor; Female; Glycerides; Intracellular Membranes; Male; Microsomes; Mitochondria; Oxidation-Reduction; Rabbits; Rats

PY - 1994

Y1 - 1994

N2 - The dissociation constants for octanoyl-CoA, dodecanoyl-CoA and hexadecanoyl-CoA binding to acyl-CoA-binding protein (ACBP) were determined by using titration microcalorimetry. The KD values obtained, (0.24 +/- 0.02) x 10(-6) M, (0.65 +/- 0.2) x 10(-8) M and (0.45 +/- 0.2) x 10(-13) M respectively, were much lower than expected. ACBP was able to extract hexadecanoyl-CoA from phosphatidylcholine membranes immobilized on a nitrocellulose membrane. The acyl-CoA/ACBP complex formed was able to transport acyl-CoA to mitochondria or microsomes in suspension, or to microsomes immobilized on a nitrocellulose membrane, and to donate them to beta-oxidation or glycerolipid synthesis in mitochondria or microsomes, respectively.

AB - The dissociation constants for octanoyl-CoA, dodecanoyl-CoA and hexadecanoyl-CoA binding to acyl-CoA-binding protein (ACBP) were determined by using titration microcalorimetry. The KD values obtained, (0.24 +/- 0.02) x 10(-6) M, (0.65 +/- 0.2) x 10(-8) M and (0.45 +/- 0.2) x 10(-13) M respectively, were much lower than expected. ACBP was able to extract hexadecanoyl-CoA from phosphatidylcholine membranes immobilized on a nitrocellulose membrane. The acyl-CoA/ACBP complex formed was able to transport acyl-CoA to mitochondria or microsomes in suspension, or to microsomes immobilized on a nitrocellulose membrane, and to donate them to beta-oxidation or glycerolipid synthesis in mitochondria or microsomes, respectively.

M3 - Journal article

C2 - 8166635

VL - 299 ( Pt 1)

SP - 165

EP - 170

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

ER -

ID: 11231390