On November 10, 1998, Hang, B.; Medina, M.; Fraenkel-Conrat, H.; Singer, B. published an article.Application of 55662-66-3 The title of the article was A 55-kDa protein isolated from human cells shows DNA glycosylase activity toward 3,N4-ethenocytosine and the G/T mismatch. And the article contained the following:
Etheno adducts in DNA arise from multiple endogenous and exogenous sources. Of these adducts we have reported that, 1,N6-ethenoadenine (εA) and 3,N4-ethenocytosine (εC) are removed from DNA by two sep. DNA glycosylases. We later confirmed these results by using a gene knockout mouse lacking alkylpurine-DNA-N-glycosylase, which excises εA. The present work is directed toward identifying and purifying the human glycosylase activity releasing εC. HeLa cells were subjected to multiple steps of column chromatog., including two εC-DNA affinity columns, which resulted in >1,000-fold purification Isolation and renaturation of the protein from SDS/polyacrylamide gel showed that the εC activity resides in a 55-kDa polypeptide. This apparent mol. mass is approx. the same as reported for the human G/T mismatch thymine-DNA glycosylase. This latter activity copurified to the final column step and was present in the isolated protein band having εC-DNA glycosylase activity. In addition, oligonucleotides containing εC·G or G/T(U), could compete for εC protein binding, further indicating that the εC-DNA glycosylase is specific for both types of substrates in recognition. The same substrate specificity for εC also was observed in a recombinant G/T mismatch DNA glycosylase from the thermophilic bacterium, Methanobacterium thermoautotrophicum THF. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Application of 55662-66-3
The Article related to ethenocytosine dna glycosylase purification, Enzymes: Separation-Purification-General Characterization and other aspects.Application of 55662-66-3
Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem