Mouse Kidney Cytidine Deaminase
نویسندگان
چکیده
منابع مشابه
Mouse Kidney Cytidine Deaminase
A nucleoside aminohydrolase was prepared in 60-fold relative purity from the nonparticulate fraction of mouse kidney by denaturation at 60”, fractionation with (NH&S04, treatment with alumina gel Cr (pH 7.5), and dialysis in 0.02 M acetate buffer (pH 4.5). The’ optimal pH was 6.5. Cytidine, deoxycytidine, and I-/3-D-arabinofuranosylcytosine were deaminated, and the respective K, values were 7.5...
متن کاملActivation-induced cytidine deaminase (AID)
Activation-induced cytidine deaminase (AID) plays an essential role in the generation of a highly competent repertoire of antibodies by participating in class switch recombination (CSR) and somatic hypermutation (SHM). After B cell stimulation by antigens, AID initiates SHM and CSR by deamination of cytidine to uridine in the variable and constant regions of Ig genes. An adverse effect of AID’s...
متن کاملCytidine Deaminase from Escherichia coli
Cytidine deaminase (cytidine aminohydrolase, EC 3.5.4.5) has been purified approximately 160-fold from extracts of Escherichia coli B. The enzyme shows constant activity between pH 6 and 11. No significant change in rate is observed when DzO replaces water as the solvent. In addition to the deamination of cytidine, the purified deaminase catalyzes slow hydrolysis of N4-methylcytidine. The enzym...
متن کاملDeaminase-Independent Inhibition of Parvoviruses by the APOBEC3A Cytidine Deaminase
The APOBEC3 proteins form a multigene family of cytidine deaminases with inhibitory activity against viruses and retrotransposons. In contrast to APOBEC3G (A3G), APOBEC3A (A3A) has no effect on lentiviruses but dramatically inhibits replication of the parvovirus adeno-associated virus (AAV). To study the contribution of deaminase activity to the antiviral activity of A3A, we performed a compreh...
متن کاملIsoenzymatic forms of human cytidine deaminase.
Cytidine deaminase (CDA) purified from human placenta revealed the presence of five isoenzymatic forms that differ only in their isoelectric point. Since human cytidine deaminase exists in two variants (CDA 1 and CDA 2) with a non-conservative amino acid substitution at codon 27, in this work we demonstrate that these two variants may combine together in vitro, giving five CDA isoforms as obser...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)93407-1