NewsRelease
HemogloBind™Employed In A NanoLC−MALDI MS/MSMethod for Identifying Single Mutation Hemoglobin Variants
MONMOUTHJUNCTION, NJ, February9, 2023 -- Biotech Support Group reports on a journal articledescribing the simplicity and efficiency of HemogloBind™, to purifyHemoglobin, in a nano LC−MALDI MS/MS measurement of single aminoacid mutations in Hb variants.
Thecitation is:
Dasauni,Pushpanjali, et al. "Optimizationand Identification of Single Mutation in Hemoglobin Variants with 2,2, 2 Trifluoroethanol Modified Digestion Method and Nano− LCCoupled MALDI MS/MS." Molecules 27.19(2022): 6357.
Hemoglobin(Hb) variants arise due to point mutations in globin chains and theirpathological treatments rely heavily on the identification of thenature and location of the mutation in the globin chains. Becausethere is high sequence homology between normal Hb and Hb variantchains, identification of variants by mass spectrometry is verydifficult and requires the full sequence coverage of α− andβ−chains. Therefore, the present study aims to develop andoptimize a specific method of sample processing that could lead toimproved sequence coverage and analysis of Hb variants by nanoLC−MALDI MS/MS.
Thearticle states “Pure Hb was isolated from hemolysate by usingHemoglobind … The Hb bound to the matrix was eluted by increasingthe pH of the buffer using 100 mM Tris borate, pH 9. This allows foreasy, one−step isolation of Hb from hemolysate.”
“Theuse of Hemoglobind reduced the time to obtain pure Hb in an easysingle–step procedure. Pure Hb protein is required specifically tooptimize and standardize methods for diagnostics. … The desorbed Hbwas compatible with LC–MS, and other proteomics studies, as weverified, did not show any change in its intact mass either. Thisone−step affinity purification gave us the utmost purified Hb.”The article concludes that a sensitive, robust, and reproduciblemethod was developed to identify/ characterize single substitutionmutations in the Hb disorder variants. It simply used pure Hbisolated from blood in a single step by using the Hemoglobind matrix,followed by TFE based sample processing and digestion by trypsin,followed by nano−LC separation. The separated peptides were spottedonto MALDI plates upon elution from a nano−LC column and subjectedto MALDI MS and MS/MS analysis. The method highlights a non−targetedapproach for the identification of Hb variants and itsreproducibility to yield 100% sequence coverage for the β−chainwith precise identification of all the mutations. It has thepotential to become a regular screening/diagnosis tool for theidentification of single amino acid mutations in Hb variants.
“Iam very pleased to see that HemogloBind™ performed so well, forsuch an important heathcare purpose. While most of the applicationsfor HemogloBind™ are for depletion, this application shows itsversatility in purifying Hemoglobin for mutational analysis. Weenvision that this and similar methods will be applicable for notonly conventional venous blood samples, but potentially dried bloodspots as well, as only small amounts of pure Hemoglobin are requiredin the final analysis.” states Swapan Roy, Ph.D., President andFounder of Biotech Support Group.
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Keywords:Hemoglobinpurification, Hemoglobin variants, Hemoglobin mutations,HemogloBind™,Hemoglobinopathies,Sicklecell disease, Thalassemia
AboutBiotech Support Group LLC
Convergingwith technological disruptions forthcoming in healthcare, BiotechSupport Group continues its growth in the consumable researchproducts area supporting the rapidly expanding installation of LC-MSinstrument and computational infrastructure. For this market, keyproducts include: AlbuVoid™ and AlbuSorb™ for albumin depletion,Cleanascite™ for lipid adsorption, HemogloBind™ and HemoVoid™for hemoglobin removal, For more information, go tohttp://www.biotechsupportgroup.com.
ForBusiness Development,contact:
MatthewKuruc 732-274-2866, [email protected]