Diversity of fatty acid-binding protein structure and function: studies with fluorescent ligands

Author(s):  
Judith Storch
1998 ◽  
Vol 92 (1) ◽  
pp. 1-25 ◽  
Author(s):  
Friedhelm Schroeder ◽  
Christopher A Jolly ◽  
Tae-Hyeon Cho ◽  
Andrey Frolov

2011 ◽  
Vol 343-344 ◽  
pp. 438-447
Author(s):  
Cheng Li Zheng ◽  
Gang Yi Xu ◽  
Dai Hua Wang

In order to understand the structure and function of H-FABP gene, reveal the effect on the heart-type fatty acid-binding protein in goat, the cDNA of H-FABP gene was cloned and sequenced from heart of Tianfu goat (an emerging breed) by T-A clone techniques. The structure and function of H-FABP were analyzed by bioinformatics, and the gene expression profile in different tissues was examined by real-time PCR. The results showed that the full sequence of H-FABP cDNA is 650 bp, containing 402 bp coding region (CDS) encoding 133 amino acids. The isoelectric point (pI) of the protein is 6.11, and the molecular weight is 14.7 kDa. There were eight phosphorylational sites in this protein. The secondary structure of the protein was mainly α-helix, random coil and extended strand structure. The deduced amino acid sequence of H-FABP shared significant identity with the H-FABP from other mammals. The phylogenic tree based on H-FABP protein sequence was detected the closest relationship to cattle. A predicted 3D model was constructed by homology modeling. H-FABP mRNA is a broad-spectrum expression gene, which was detected in heart, liver, spleen, lung, kidney, longissimus muscle and leg muscle. In particular, high expression levels of H-FABP mRNA were detected in heart, longissimus muscle and leg muscle, but low expressions were observed in liver tissue.


2011 ◽  
Vol 95 (8) ◽  
pp. 2749-2752.e5 ◽  
Author(s):  
Zhen Tian ◽  
Zhen-Ao Zhao ◽  
Xiao-Huan Liang ◽  
Xiu-Hong Zhang ◽  
Ai-Guo Sha ◽  
...  

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