Biochemistry, comparative transport

Hansen, H.J.M. (1987). Comparative studies on lipid metabolism in various salt-transporting organs of the European eel (Anguilla anguilla). Mono-unsaturated phosphatidyl ethanolamine as a key substance. Comparative Biochemistry and Physiology 88B, 323-332. 

Hansen, H.J.M., Olsen, A.G. and Rosenkilde, P. (1995). Formation of phosphatidyl ethanolamine as a putative regulator of salt transport in the gills and oesophagus of the rainbow trout (Oncorhynchus mykiss). Comparative Biochemistry and Physiology 112B, 161-167. 

Smith, M.W. and Ellory, J.C. (1971). Temperature-induced change in Na transport and ATPase in goldfish. Comparative Biochemistry and Physiology 39A, 209-218. 

Cheah, K. S. Bryant, C. (1966). Studies on the electron transport system of Moniezia expansa (Cestoda). Comparative Biochemistry and Physiology, 19 197-223. 

Murphy, W. A. Lumsden, R. D. (1984a). Phloretin inhibition of glucose transport by the tapeworm Hymenolepis diminuta a kinetic analysis. Comparative Biochemistry and Physiology, 78A 749-54. 

The properties and biological importance of the transferrins can be expected to continue to generate expanding interest on the part of both physical and biological scientists. The many provocative facets of the comparative and genetic biochemistry should be obvious. Functionally, the serum transferrin is one of the few examples of a protein whose function is to chelate a metal ion in order to transport the metal ion rather than to form a catalytic complex with it. Not only must the transferrin form the complex and transfer the metal, but it must also release the... 

Rosen, B.P. 2002. Transport and detoxification systems for transition metals, heavy metals and metalloids in eukaryotic and prokaryotic microbes. Comparative Biochemistry and Physiology—A Molecular and Integrative Physiology, 133 689-93. 

The area of membrane transport has always been an interdisciplinary field. Physiologists, biochemists, biophysicists, cell biologists and pharmacologists have all made their contributions to the development of our knowledge in this field, often in collaborative studies. The appearance of this book in the series New Comprehensive Biochemistry is justified perhaps more by the future contributions to be expected from fundamental biochemistry than by the contributions made by biochemistry so far. Our biochemical understanding of the molecular structure and dynamics of the various transport systems is still in a primitive state compared to that for biomolecules like nucleic acids and water-soluble proteins. The editors hope that the publication of this volume may arouse the interest of many biochemists, especially the younger ones, for this field of biochemistry and thus contribute to its development. 

The activation of molecular oxygen by transition metal complexes is of fundamental interest for chemistry, biology, and medicine. As it is well known from biochemistry, iron is crucial in the transportation, storage, and activation of oxygen, and with respect to these processes only copper is of comparable relevance. 

Cytochrome c (see 2 and Fig. 2-7) in the mitochondria is part of the chain of electron carrier proteins that ultimately produce ATP from ADP (oxidative phosphorylation). In principle, the heme in cytochrome c is the same as that in hemoglobin. But in detail, the vinyl groups, after conversion to thioethers, are covalently linked to cysteine amino residues of the protein chain [2,5]. The fifth coordination site of iron is occupied again by the imidazole N-atom of a histidine, but the sixth position is now coordinated to the S-atom of a methionine (Figs. 2-7, 2-17). The redox potential of low-spin Fe(III)/Fe(II) with E°= +0.25 V vs. NHE is drastically altered compared to heme. Now this heme iron is much more able to act in the electron-transporting chain by redox cycling. The mechanisms of electron transfer are available in modem textbooks of biochemistry. It is interesting to note that the macromolecular protein chain... 

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