NewsRelease

JournalArticle Cites HemoVoid™ in Post-translational Changes in Red CellProteomic Study

MONMOUTHJUNCTION, NJ, February 13, 2020 -- BiotechSupport Group reports on a recent journal article describing thesimplicity and efficiency of their hemoglobin depletion technologyfor enriching the red cell proteome, to study post-translationalmodifications in erythrocytic diseases. 

Thecitation is:

Bollenbach,Alexander, et al. "GC-MSand LC-MS/MS pilot studies on the guanidine (NG)-dimethylation innative, asymmetrically and symmetrically NG-dimethylatedarginine-vasopressin peptides and proteins in human red bloodcells." Journalof Chromatography B (2020):122024.

Protein-argininemethyltransferases catalyze the methylation of the guanidine (NG)group of proteinic L-arginine (Arg) to produce monomethyl anddimethylarginine proteins. Upon proteolysis, free amino acidsmonomethylarginine (MMA), symmetric dimethylarginine (SDMA) andasymmetric dimethylarginine (ADMA), respectively are released.Previous studies showed that human red blood cells are rich in large(> 50 kDa) ADMA-containing proteins of unknown identity. The studyaimed to report the Identity, biological activity and concentrationof NG-methylatedproteins by using GC-MS and LCMS/MS approaches. The article states“we included in our method the use of HemoVoid cartridges to removespecifically most erythrocytic hemoglobin and to improve the SDS-PAGEseparation of proteins for further processing. The HemoVoidcartridges, … allowed removal of erythrocytic hemoglobin to a largeextent from the hemolysate. … removal of hemoglobin by thistechnique enabled an effective separation by SDS-PAGE and isolationof bands, presumably by avoiding overloading of the gels byhemoglobin.”. The article concludes that the LC-MS/MS proteomicstudy identified several membrane and cytosolic erythrocyticNG-dimethylatedproteins, including spectrin-α (280 kDa), spectrin-β (247 kDa) andprotein 4.1 (80 kDa). Furthermore, that the newly identified maintargets for NG-dimethylationin human erythrocytes should be given a closer look in erythrocyticdiseases like hereditary spherocytosis.

“Asred cells do not have a nucleus, they do not produce new proteinsthroughout their existence. So proteomic changes within red cells areoften as a result of post-translational modifications. To study thesechanges, the large quantity of hemoglobin presents background noisewhich can interfere with these investigations. So it is satisfying tosee how HemoVoid™. can help in these analyses as post-translationalchanges within red cells might be used in the future as biomarkersfor disease”, states Swapan Roy, Ph.D., President and Founder ofBiotech Support Group.

Formore information on HemoVoid™, visit:

http://www.biotechsupportgroup.com/HemoVoid-Hemoglobin-Depletion-From-Erythrocytes-p/hvk.htm

Formore information of all of our Hemoglobin removal products, visit:

https://www.biotechsupportgroup.com/Articles.asp?ID=452

AboutBiotech Support Group LLC

Convergingwith cultural and technological disruptions forthcoming inhealthcare, Biotech Support Group develops methods for cost effectiveand efficient sample prep essential for these expanding markets.Following a tiered business strategy, the company continues itsgrowth in the consumable research products area supporting therapidly expanding installation of LC-MS instrument and computationalinfrastructure. For this market, key products include: AlbuVoid™and AlbuSorb™ for albumin depletion, Cleanascite™ for lipidadsorption, HemogloBind™ and HemoVoid™ for hemoglobin removal,and NuGel™ for functional proteomics. From these innovations, thecompany has acquired knowledgebase and biomarker intellectualproperty assets that support discoveries of protein markers fromblood, with special emphasis on early detection and personalizedmedical decisions for cancer patients. For more information, gotohttp://www.biotechsupportgroup.com

Contact:
MatthewKuruc 732-274-2866, [email protected]