@2024 Afarand., IRAN

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ISSN: 2252-0805    The Horizon of Medical Sciences 2014;20(1):1-7

Background
Glycation is non-enzymatic reaction of adding sugars to proteins, which goes on to form color full and fluorescence species with cross-joints named as AGE [5]. Fructose has tendency to form AGEs 8 to 10 times more than glucose does [6]. Aspirin is non-steroidal anti-inflammatory drug [7]. Melittin and phospholipase-A2 are two main components of bee venom [11]. There are various agents, which inhibit glycation in a manner. Lysine amino acid competes with amine protein group in binding to the sugar [14]; and aspirin connects with protein and inhibits sugar to reach amine factor [15].Some anti-oxidants, like bee venom, decrease glycation through glyco-oxidation.
Previous Studies
Non-declared
Aim(s)
The aim of the study was to assess anti fructation effect of bee venom, in comparison with aspirin.
Research type
The method is empirical.
Research society, place and time
Research society was the population of healthy and non-smoking persons.
Sampling method and number
According to Austen Riggs protocol [16], hemoglobin of healthy and non-smoking persons was extracted, and then, using Bradford method [17] and ultraviolet spectrometry, its concentration was determined. Bovine serum albumin (BSA) protein was used as standard protein. 10 mg per ml hemoglobin was incubated at the presence and absence of 40 mMol fructose for 5 weeks at 37℃ on shaker with 40 rpm velocity. To evaluate bee venom and aspirin’s effect, hemoglobin was fructated at the presence of these two materials. To study releasing value of heme group and hemoglobin’s soret band changes, protein and visible-ultraviolet spectrometry method were used, respectively. Value of free amines in hemoglobin was measured during fructation and at the presence of aspirin and bee venom, using method of changes in the florescamin fluorescence emission. To compute free amine percent, the equation [(alone hemoglobin fluorescence emission/ hemoglobin fluorescence emission at desired conditions)*100] was used. Spectro-polarimeter and circular bicolor spectrometry method (CD) were used to consider fructed hemoglobin protein structure changes. Samples were considered on the interval between 190 and 260 nm wavelengths.
Used devices&materials
UV-3100 (Shimadzu; Japan) visible-ultraviolet spectrometer, Merk (Germany) fructose, bee venom (Islamic Azad University, Sciences and Research Branch; Iran), aspirin (Sigma; USA), spectro-polarimeter (AVIV; USA) were used. Method of changes in the florescamin fluorescence emission was performed with Sigma (USA). To compute each second structure of protein, CDNN software was used [19]. Data were analyzed, using InStat 3 software and One-way Variance Analysis statistical tests.
Findings by Text
Visible-ultraviolet spectrometry: At the presence of hemoglobin, hemoglobin incubation resulted in decrease in soret band of fructed hemoglobin absorption than hemoglobin does. In a concentration-dependent procedure, bee venom increased absorption. There was no significant difference between increase in absorption at the presence of 40 micrograms per milliliter bee venom and decrease in fructation at the presence of aspirin (Diagram 1). Fluorescence spectrometry: There was no significant difference between value of free amines at the presence of 20 and 40 microgram per milliliter bee venom and value of free amines at the presence of aspirin (Diagram 2). Circular bicolor spectrometry: During fructation and in a concentration-dependent procedure, bee venom prevented change in the second structure of hemoglobin. Aspirin, also, inhibited these changes, and it decreased significantly fructation as well as its followed up structure changes (Diagram 3). Fructation resulted in decrease in alpha helix in hemoglobin and, subsequently, increase in beta plates. Bee venom and aspirin had a significant effect in inhibition of these changes. 40 micrograms per milliliter bee venom had an approximately similar function with aspirin concerning inhibition of hemoglobin fructation and structure changes induced by it (Table 1).
Main comparison to the similar studies
Based on the results of a study, hemoglobin glycation results in decrease in soret absorption peak and its displacement [22], which is fully consistent with the results of the present study.
Suggestions
Non-declared
Limitations
Non-declared
Conclusions
Fructation results in induction of structure changes in hemoglobin. Like aspirin, bee venom can inhibit formed changes in hemoglobin caused by fructation.
Acknowledgments
Researchers feel grateful to Research Deputy of Kharazmi University.
Conflict of interest
Non-declared
Ethical Permissions
Non-declared
Funding Sources
Research Deputy of Kharazmi University funded the study.

TABLES and CHARTS

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