Acetohexamide - CAS 968-81-0
Not Intended for Therapeutic Use. For research use only.
Product Name:
Catalog Number:
1-((p-Acetylphenyl)sulfonyl)-3-cyclohexyl-ure;4-Acetyl-n-((cyclohexylamino)carbonyl)-benzenesulfonamid;Dymelor; Acetohexamid;Gamadiabet;Dimelin;Dimelor;1-(4-Acetylphenyl)sulfonyl-3-cyclohexylurea;Hypoglicil;Metaglucina;Minoral;N-(p-Acetylphenylsulfonyl)-N'-cyclohexylurea;Ordimel;Tsiklamid;U 14812
CAS Number:
Acetohexamide, a sulfonylurea derivative, is a first-generation sulfonylurea medication used to treat diabetes mellitus type 2, particularly in people whose diabetes cannot be controlled by diet alone. It is a hyopglycemic agent with moderate uricosuric activity. It stimulates the pancreas to secrete insulin and is used as an oral hypoglycemic agent. It was developed by Eli Lilly and Company and has been listed.
Molecular Weight:
Molecular Formula:
Grams to Kilograms
Quality Standard:
In-house standard
Canonical SMILES:
Current Developer:
Acetohexamide was developed by Eli Lilly and Company and has been listed.
Chemical Structure
CAS 968-81-0 Acetohexamide

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Reference Reading

1.Analysis of free drug fractions in human serum by ultrafast affinity extraction and two-dimensional affinity chromatography.
Zheng X1, Podariu M1, Matsuda R1, Hage DS2. Anal Bioanal Chem. 2016 Jan;408(1):131-40. doi: 10.1007/s00216-015-9082-7. Epub 2015 Oct 13.
Ultrafast affinity extraction and a two-dimensional high performance affinity chromatographic system were used to measure the free fractions for various drugs in serum and at typical therapeutic concentrations. Pooled samples of normal serum or serum from diabetic patients were utilized in this work. Several drug models (i.e., quinidine, diazepam, gliclazide, tolbutamide, and acetohexamide) were examined that represented a relatively wide range of therapeutic concentrations and affinities for human serum albumin (HSA). The two-dimensional system consisted of an HSA microcolumn for the extraction of a free drug fraction, followed by a larger HSA analytical column for the further separation and measurement of this fraction. Factors that were optimized in this method included the flow rates, column sizes, and column switching times that were employed. The final extraction times used for isolating the free drug fractions were 333-665 ms or less.
2.Chromatographic studies of changes in binding of sulfonylurea drugs to human serum albumin due to glycation and fatty acids.
Basiaga SB1, Hage DS. J Chromatogr B Analyt Technol Biomed Life Sci. 2010 Nov 15;878(30):3193-7. doi: 10.1016/j.jchromb.2010.09.033. Epub 2010 Oct 23.
This report examines the use of high-performance affinity chromatography as a screening tool for studying the change in binding by sulfonylurea drugs to the protein human serum albumin (HSA) during diabetes. The effects of both the non-enzymatic glycation of HSA and the presence of fatty acids on these interactions were considered using a zonal elution format. It was found that there was a significant increase (i.e., 2.7- to 3.6-fold) in the relative retention of several sulfonylurea drugs (i.e., acetohexamide, tolbutamide, glybenclamide and gliclazide) on columns containing normal versus glycated HSA. The addition of various long chain fatty acids to the mobile phase gave the same trend in retention for the tested drugs on both the HSA and glycated HSA columns, generally leading to lower binding. Most of the fatty acids examined produced similar or moderately different relative shifts in retention; however, palmitic acid was found to produce a much larger change in retention on columns containing glycated HSA versus normal HSA under the conditions used in this study.
3.Molecular and biochemical characterisation of human short-chain dehydrogenase/reductase member 3 (DHRS3).
Lundová T1, Zemanová L2, Malčeková B3, Skarka A4, Štambergová H5, Havránková J6, Šafr M7, Wsól V8. Chem Biol Interact. 2015 Jun 5;234:178-87. doi: 10.1016/j.cbi.2014.10.018. Epub 2014 Oct 29.
Dehydrogenase/reductase (SDR family) member 3 (DHRS3), also known as retinal short-chain dehydrogenase/reductase (retSDR1) is a member of SDR16C family. This family is thought to be NADP(H) dependent and to have multiple substrates; however, to date, only all-trans-retinal has been identified as a DHRS3 substrate. The reductive reaction catalysed by DHRS3 seems to be physiological, and recent studies proved the importance of DHRS3 for maintaining suitable retinoic acid levels during embryonic development in vivo. Although it seems that DHRS3 is an important protein, knowledge of the protein and its properties is quite limited, with the majority of information being more than 15 years old. This study aimed to generate a more comprehensive characterisation of the DHRS3 protein. Recombinant enzyme was prepared and demonstrated to be a microsomal, integral-membrane protein with the C-terminus oriented towards the cytosol, consistent with its preference of NADPH as a cofactor.
4.Detection of heterogeneous drug-protein binding by frontal analysis and high-performance affinity chromatography.
Tong Z1, Joseph KS, Hage DS. J Chromatogr A. 2011 Dec 9;1218(49):8915-24. doi: 10.1016/j.chroma.2011.04.078. Epub 2011 May 6.
This study examined the use of frontal analysis and high-performance affinity chromatography for detecting heterogeneous binding in biomolecular interactions, using the binding of acetohexamide with human serum albumin (HSA) as a model. It was found through the use of this model system and chromatographic theory that double-reciprocal plots could be used more easily than traditional isotherms for the initial detection of binding site heterogeneity. The deviations from linearity that were seen in double-reciprocal plots as a result of heterogeneity were a function of the analyte concentration, the relative affinities of the binding sites in the system and the amount of each type of site that was present. The size of these deviations was determined and compared under various conditions. Plots were also generated to show what experimental conditions would be needed to observe these deviations for general heterogeneous systems or for cases in which some preliminary information was available on the extent of binding heterogeneity.