Adenine ribo- and deoxyribonucleotide metabolism in human erythrocytes, B- and T-lymphocyte cell lines, and monocyte-macrophages.

Adenine ribo- and deoxyribonucleotide metabolism in human erythrocytes, B- and T-lymphocyte cell lines, and monocyte-macrophages.
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人红细胞、B 淋巴细胞和 T 淋巴细胞系以及单核巨噬细胞中的腺嘌呤核糖核苷酸和脱氧核糖核苷酸代谢。

DOI:
10.1073/pnas.82.19.6682
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发表时间:
1985
影响因子:
11.1
通讯作者:
Brockway,R
Brockway,R
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Valentine,WN;Paglia,DE;Clarke,S;Morimoto,BH;Nakatani,M;Brockway,R

文献摘要

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腺嘌呤脱氧核糖核苷酸通常包装在DNA中,在腺苷脱氨酶(腺苷氨基水解酶,EC 3.5.4.4)缺乏时优先浓缩在红细胞和淋巴细胞胞质溶胶中。一个频谱的胞质酶活性的反应速度,K0.5s,核苷酸分区与核糖和脱氧核糖核苷酸孵育后定义。AMP和dAMP在体外被脱磷酸化,但只有AMP被脱氨基。虽然核苷酸酶活性在淋巴细胞中强得多,但在指定条件下,AMP脱氨酶是所有红细胞和淋巴细胞裂解物中的主要降解反应。对于大多数胞质酶,核糖核苷酸的首选辅因子,这意味着dADP和dATP往往可能是旁观者在代谢事件。腺苷酸激酶介导的分区约等摩尔的核糖和脱氧核糖核苷酸底物产生了一个非常大的优势AMP的单磷酸盐室,单磷酸盐单独直接容易受到降解损失。淋巴细胞的腺苷酸激酶(S)显着不同的反应速度与核苷酸辅因子,K0.5s,并在底物抑制的敏感性从红细胞。
Ordinarily packaged in DNA, adenine deoxyribonucleotides are preferentially concentrated in erythrocyte and lymphocyte cytosol in adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4) deficiency. A spectrum of cytosol enzyme activities are defined in terms of reaction velocities, K0.5s, and nucleotide partition after incubation with ribo- and deoxyribonucleotides. AMP and dAMP were dephosphorylated, but only AMP was deaminated in vitro. Although nucleotidase activity is much stronger in lymphocytes, AMP deaminase was the dominant degradative reaction in all erythrocyte and lymphocyte lysates under the conditions specified. For most cytosolic enzymes, ribonucleotides were preferred cofactors, implying that dADP and dATP often may be bystanders at metabolic events. The adenylate kinase-mediated partition of approximately equimolar ribo- and deoxyribonucleotide substrates yielded a very large preponderance of AMP in the monophosphate compartment, the monophosphates alone being directly vulnerable to degradative loss. The adenylate kinase(s) of lymphocytes differed strikingly from those of erythrocytes in reaction velocities with nucleotide cofactors, K0.5s, and in susceptibility to substrate inhibition.