Fish proteins structure, separation

Based on previous works on Homeopathy we have hypothesized that the primary target of a homeopathic potency in an organism is the water-channel protein or aquaporin (Sukul and Sukul, 2001). Aquaporins occur in all life forms and facilitate permeation of water across biological membranes. We have discussed in details about the structure and function of aquaporins and their relation to health and disease in chapter IV. There are several types of aquaporins (AQP) and one type AQP1 occurs abundantly in red blood cells of vertebrates. If the primary target of a homeopathic potency is aquaporin, application of a homeopathic potency on cell membranes would affect water flow into the cells. In order to test this hypothesis we treated red blood cells of a fresh water fish (Clarius batrachus) with Mercuric chloride 30 (Merc cor 30) and Nux vomica 30 (Nux vom 30) separately in a hypotonic medium. In the control red cells were treated with Ethanol 30. The diluent medium in all the three potencies consisted of 90% ethanol and 10% distilled water. 

The analyses carried out up to now on such extracts have been based upon differences of solubility (see p. 235). The discussion of the results obtained has made clear that a reinvestigation of these mixtures is necessary in order to define more accurately the structure proteins of fish muscle. Electrophoresis, which permits the analysis of such mixtures with a minimum of alteration, appears a particularly suitable method. It has been applied as yet only to carp muscle extracts of high ionic strength (Hamoir, 1951b, 1954, 1955). In view of the very constant electrochemical behavior of the muscle structure proteins (see Hamoir, 1953a), it seems safe to assume that similar results will be obtained with other fishes. The results already obtained will therefore be more extensively described. The slight difference in extractibility previously mentioned between white and red rabbit muscles (Crepax, 1952) suggests that a separate study of both fish muscles would also be desirable in this case, but it has not yet been undertaken. 

With the exception of structural proteins, which often remain linear, the polypeptide chains of proteins usually fold into complex, three-dimensional conformations. In enzymes, these conformations bring together certain functional groups of amino acids that are distantly located in the chain, so as to delimit specific binding sites and catalytic centers, disposed in such a manner that reaction substrates are fished out from the surrounding medium, immobilized in a particular configuration, and caused to interact. In addition, many enzymes also bear separate sites, called allosteric, which bind regulatory substances that modify the enzyme s functional properties. 

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