MONMOUTH JUNCTION, N.J. - Feb. 15, 2020 -Biotech Support Group reports on a recent journal article describing the simplicity and efficiency of their hemoglobin depletion technology for enriching the red cell proteome, to study post-translational modifications in erythrocytic diseases.

The citation is:

Bollenbach, Alexander, et al. "GC-MS and LC-MS/MS pilot studies on the guanidine (NG)-dimethylation in native, asymmetrically and symmetrically NG-dimethylated arginine-vasopressin peptides and proteins in human red blood cells. (https://www.sciencedirect.com/science/article/abs/pii/S1570023219316216)" Journal of Chromatography B (2020): 122024.

Protein-arginine methyltransferases catalyze the methylation of the guanidine (NG) group of proteinic L-arginine (Arg) to produce monomethyl and dimethylarginine proteins. Upon proteolysis, free amino acids monomethylarginine (MMA), symmetric dimethylarginine (SDMA) and asymmetric 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 study aimed to report the Identity, biological activity and concentration of NG-methylated proteins by using GC-MS and LCMS/MS approaches. The article states "we included in our method the use of HemoVoid cartridges to remove specifically most erythrocytic hemoglobin and to improve the SDS-PAGE separation of proteins for further processing. The HemoVoid cartridges, … allowed removal of erythrocytic hemoglobin to a large extent from the hemolysate. … removal of hemoglobin by this technique enabled an effective separation by SDS-PAGE and isolation of bands, presumably by avoiding overloading of the gels by hemoglobin.". The article concludes that the LC-MS/MS proteomic study identified several membrane and cytosolic erythrocytic NG-dimethylated proteins, including spectrin-α (280 kDa), spectrin-β (247 kDa) and protein 4.1 (80 kDa). Furthermore, that the newly identified main targets for NG-dimethylation in human erythrocytes should be given a closer look in erythrocytic diseases like hereditary spherocytosis.




"As red cells do not have a nucleus, they do not produce new proteins throughout their existence. So proteomic changes within red cells are often as a result of post-translational modifications. To study these changes, the large quantity of hemoglobin presents background noise which can interfere with these investigations. So it is satisfying to see how HemoVoid™. can help in these analyses as post-translational changes within red cells might be used in the future as biomarkers for disease", states Swapan Roy, Ph.D., President and Founder of Biotech Support Group.

For more information on HemoVoid™, visit:
http://www.biotechsupportgroup.com/HemoVoid-Hemoglobin-Depletion-From-Erythrocytes-p/hvk.htm

For more information of all of our Hemoglobin removal products, visit:
https://www.biotechsupportgroup.com/Articles.asp?ID=452

Contact:
Matthew Kuruc 732-274-2866, mkuruc@biotechsupportgroup.com

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