Author: Vinay S. Mahajan; Faisal Alsufyani; Hamid Mattoo; Ian Rosenberg; Shiv Pillai
Title: Alterations in sialic-acid O-acetylation glycoforms during murine erythrocyte development Document date: 2018_11_14
ID: dsflny30_6
Snippet: Despite the loss of 9-O-acetylation on erythrocytes, there was no evidence of anemia or other obvious change in RBC physiology. Surprisingly, Casd1-deficient erythrocytes, which lack 9-O-acetyl sialic acid based on the lack of binding to CHE-FcD, also lost reactivity to TER-119, suggesting that this antibody may recognize a 9-O-acetyl sialic acid glyco-epitope (Fig 3A) . A previous study on the identification of the target of TER-119 suggested th.....
Document: Despite the loss of 9-O-acetylation on erythrocytes, there was no evidence of anemia or other obvious change in RBC physiology. Surprisingly, Casd1-deficient erythrocytes, which lack 9-O-acetyl sialic acid based on the lack of binding to CHE-FcD, also lost reactivity to TER-119, suggesting that this antibody may recognize a 9-O-acetyl sialic acid glyco-epitope (Fig 3A) . A previous study on the identification of the target of TER-119 suggested that this antibody can immunoprecipitate proteins of 110 kDa, 60 kDa, 52 kDa and 32 kDa from the erythrocyte membrane (Kina et al., 2000) . Of these, only the 52 kDa protein was detectable in a Western Blot using TER-119. However, the identity of this protein was not deciphered, and it was suspected to be a glycophorin A associated molecule.
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