Extreme dilutions of mercuric chloride produce longer binding interaction with ?-amylase as compared to blank solvents
Mondal, Priya; Chakraborty, Indrani; Sukul , Nirmal Chandra; Konar, Atheni; Sarkar, Tandra; Sukul , Anirban.
Int. j. high dilution res
; 19(3): 18-26, 2020.
Artigo
em Inglês
| LILACS, HomeoIndex (homeopatia) | ID: biblio-1146524
Background:
High and ultra-low doses of HgCl2modulate α-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 α-amylase without intervention of its substrate starch. (ii) To see whether the MT and UHDs produce longer binding interaction with α-amylase than the control.Methods:
Mercuric chloride MT (0.15 M) or Merc corθ 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 α-amylase at 250C and the reaction was observed for 33.3 min.Results:
While Merccorθ produced endothermic reaction, all other ligands did exothermic reaction. All ligands sustained heat change for the entire period of observation (33.3 min).Conclusions:
Merc corθ and potencies produced exactly the opposite reaction at the protein binding sites. Merc cor200 cH and 1000 cH produced highest heat change (6 micro cal/sec) during interaction with α-amylase.(AU)
Biblioteca responsável:
BR926.1
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