直流による蛋白質疎水結合の回復

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It would be possible to assume that the senility of living individuals comes from very minute denaturation on each protein of all kinds, that is enzme, nucleus and membrane etc. which organize the cell. Then it would be able to infer that each living individuals must be bound with 2nd Law and be within closed system, not the opened, as generally natural chemical phenomena obey the Law. In aqueous solutjon the velocity of catalitic action by inorganic or metalic ions (e. g. by Cu^<++> to H_2 O_2 decomposition) is enhanced when the concntration of NaCl in the soluion is increased. This experimental result suggests that the active center in an enzyme will be activated by the protein, which occupies the most part of enzyme and has inside itself the numerous plus and minus fixed ions. And it is suggested that in aqueous solution the fixed ions held in the protein of enzyme will make up dense electrostatic field which is resemble to the field made by all kinds of chemical ligands around metal ion. And then, if the hydrophobic-bond of protein, especially of enzyme, would become slack by some condition or cause, it is possible to presume that the activity of the protein will diminish owing to decreasing the density of fixed ions inside the molecules. During the research of paper electrophoresis, it happened to be found that the fraction of amino-acids contracts by direct current when the pH of the electrolyte in paper comes near to the amino-acid's isoelectric point. Standing upon this electrical phenomenon, the protein which is the same amphoteric electrolyte as amino-acids must contract itself by D. C.. Therefor in this study the effect caused by D. C. to the hydrophobic-bond of proteins was researched and discussed. Simple gelatine solution decreases its viscosity when it is electrified by D. C., and this effect means that each gelatine molecule contracts itself as expected of abovementioned phenomenon. The activity of α-amylase diminishes when it was put into the rich gelatine solution, and the cause of which is conjectured as owing to slackening of the enzyme's hydrophobic-bond. High concentratin of protein is supposed as it weakens the potential energy of aqueous molecule and becomes the cause of the slackeing of amylase. In conclusion, when the compound solution of 10% gelatine and 0.02% α-amylase was electrified and the viscosity of the solution decreased as well as simple gelatine solution, the recovery of hydrophbic-bond of amylase is expected comming from the increase of aqua's potential which is accompanied with contracting of gelatine. But at the present condition the revival of α-amylase by D. C. is not yet observed except only one case using one kind of coarse gelatine.
大分県立芸術文化短期大学の論文
1966-12-10

直流による蛋白質疎水結合の回復

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