Extreme dilutions of mercuric chloride produce longer binding interaction with ?-amylase as compared to blank solvents
Background High and ultra low doses of HgCl2 modulate ?-amylase starch interaction through two different binding sites of the enzyme. Mercurius corrosivus at ultra high dilution (UHD) is reported to have a long duration of action for 30-60 days. Objectives (i) To see whether the mother tincture and...
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Published in | International journal of high dilution research Vol. 19; no. 3; pp. 18 - 26 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
02.04.2021
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Online Access | Get full text |
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Summary: | Background
High and ultra low doses of HgCl2 modulate ?-amylase starch interaction through two different binding sites of the enzyme. Mercurius corrosivus at ultra high dilution (UHD) is reported to have a long duration of action for 30-60 days.
Objectives
(i) To see whether the mother tincture and UHDs of mercuric chloride could directly act on ?-amylase without intervention of its substrate starch. (ii) To see whether the MT and UHDs produce longer binding interaction with ?-amylase than the control.
Methods
Mercuric chloride MT (0.15 M) or Merc cor ? and its three UHDs, 30, 200, 1000 cH called potencies were in 90% ethanol. Blank 90% ethanol and deionised and distilled (DD) water were used as controls. All ethanol based ligands were diluted with DD water to reduce EtOH content to 0.09%. Using an ITC instrument each ligand was injected once at 10 µl into15µM ?-amylase at 25 0C and the reaction was observed for 2000 s.
Results
While Merc cor ? produced endothermic reaction, all other ligands did exothermic reaction. Water control and blank ethanol maintained post injection heat change up to 1200 sec. All other ligands sustained heat change for the entire period of observation (2000 sec).
Conclusions
Merc cor ? and potencies produced exactly the opposite reaction at the protein binding sites. The reaction was short-lived with water control and blank ethanol, but prolonged with Merc cor ? and potencies. Merc cor 200 cH and 1000 cH produced highest heat change (6 µl/sec) during interaction with ?-amylase. |
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ISSN: | 1982-6206 1982-6206 |
DOI: | 10.51910/ijhdr.v19i3.1015 |