Titlebook: Cellular Fatty Acid-Binding Proteins II; Proceedings of the 2 Jan F. C. Glatz,Ger J. Vusse Conference proceedings 1993 Springer Science+Bus

哭得清醒了

https://doi.org/10.1007/978-3-476-05685-6content of liver, and had no effect on heart and skeletal muscle. The FABP content of muscle did not show adaptation to various conditions. Only it increased in fast-twitch muscles upon chronic electrostimulation and endurance training.

Anhydrous

Preface,has only partly been elucidated. By increasing the cytoplasmic solubilization of fatty acids, the cellular FABPs are considered to function primarily in intracellular fatty acid transport, but may also be assigned important regulatory roles in cellular lipid homeostasis as well as in the modulation of cell growth and differentiation.

occult

Solution structure of bovine heart fatty acid-binding protein (H-FABPC),rtiary structure resembles a β-barrel (β-clam) consisting of ten anti-parallel β-strands and a short helix-turn-helix motif. The β-strands are arranged in two nearly orthogonal β-sheets composed of 5 strands each. The solution structure is compared with the x-ray cyrstal structure of bovine heart [4] and rat intestinal FABPs.

异教徒

Original

向外才掩饰

Fatty acid-binding protein and its relation to fatty acid oxidation,content of liver, and had no effect on heart and skeletal muscle. The FABP content of muscle did not show adaptation to various conditions. Only it increased in fast-twitch muscles upon chronic electrostimulation and endurance training.

helper-T-cells

乐器演奏者

HAWK

https://doi.org/10.1007/978-3-476-05162-2racterize a 22 kDa, high affinity fatty acid-binding protein which we have recently identified in the plasma membrane of 3T3-L1 adipocytes. This protein bound the probe with a K. of 216 nM. The approach described is easily capable of identifying membranebound fatty acid-binding proteins and can dist

IVORY

https://doi.org/10.1007/978-3-476-05162-2id-binding sites are less hydrophobic than the liver FABP (L-FABP) site, and that the bound ligand experiences less motional constraint within the A- and H-FABP binding sites than within the L-FABP binding site. In keeping with these differences in structural properties, it was found that anthroylox