Fatty Acid Binding Proteins and Their Roles in Transport of Long-Chain Polyunsaturated Fatty Acids across the Feto-Placental Unit

Author(s):  
Asim K. Duttaroy
2009 ◽  
Vol 126 ◽  
pp. S240
Author(s):  
Noriko Osumi ◽  
Miho Matsumata ◽  
Nobuyuki Sakayori ◽  
Motoko Maekawa ◽  
Takeo Yoshikawa ◽  
...  

Lipids ◽  
2007 ◽  
Vol 43 (1) ◽  
pp. 1-17 ◽  
Author(s):  
Friedhelm Schroeder ◽  
Anca D. Petrescu ◽  
Huan Huang ◽  
Barbara P. Atshaves ◽  
Avery L. McIntosh ◽  
...  

1991 ◽  
Vol 286 (1) ◽  
pp. 300-309 ◽  
Author(s):  
Gyorgy Nemecz ◽  
Timothy Hubbell ◽  
John R. Jefferson ◽  
John B. Lowe ◽  
Friedhelm Schroeder

2015 ◽  
Vol 57 (2) ◽  
pp. 219-232 ◽  
Author(s):  
Adriana Esteves ◽  
Anja Knoll-Gellida ◽  
Lucia Canclini ◽  
Maria Cecilia Silvarrey ◽  
Michèle André ◽  
...  

Biochemistry ◽  
1990 ◽  
Vol 29 (40) ◽  
pp. 9305-9311 ◽  
Author(s):  
Margo G. Wootan ◽  
Nathan M. Bass ◽  
David A. Bernlohr ◽  
Judith Storch

1990 ◽  
Vol 265 (3) ◽  
pp. 849-855 ◽  
Author(s):  
J T Rasmussen ◽  
T Börchers ◽  
J Knudsen

Bovine and rat liver acyl-CoA-binding proteins (ACBP) were found to exhibit a much higher affinity for long-chain acyl-CoA esters than both bovine hepatic and cardiac fatty-acid-binding proteins (hFABP and cFABP respectively). In the Lipidex 1000- as well as the liposome-binding assay, bovine and rat hepatic ACBP effectively bound long-chain acyl-CoA ester, h- and c-FABP were, under identical conditions, unable to bind significant amounts of long-chain acyl-CoA esters. When FABP, ACBP and [1-14C]hexadecanoyl-CoA were mixed, hexadecanoyl-CoA could be shown to be bound to ACBP only. The experimental results give strong evidence that ACBP, and not FABP, is the predominant carrier of acyl-CoA in liver.


1989 ◽  
Vol 21 (4) ◽  
pp. 407-418 ◽  
Author(s):  
Roger A. Peeters ◽  
Monique A.P.M. in't Groen ◽  
Marielle P. de Moel ◽  
Herman T.B. Van Moerkerk ◽  
Jacques H. Veerkamp

Sign in / Sign up

Export Citation Format

Share Document