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离体大鼠肝细胞中的嘌呤代谢

Purine metabolism in isolated rat hepatocytes.

作者信息

Smith C M, Rovamo L M, Kekomäki M P, Raivio K O

出版信息

Can J Biochem. 1977 Nov;55(11):1134-9. doi: 10.1139/o77-169.

DOI:10.1139/o77-169
PMID:922548
Abstract

The metabolism of adenine, hypoxanthine, guanine, and adenosine was studied in rat liver cell suspensions, prepared by collagenase perfusion. Oxygen supply was a critical variable in the preparation and subsequent incubationof the cells, as judged on the basis of the ratio of radioactivity in ATP to that in ADP after incubation with [14C]adenine. This ratio is suggested as an additional criterion of cell function. Adenine nucleotides synthesized from [14C]adenine were slowly catabolized to allantoin, with little incorporationof radioactivity into other purine compounds. [14C]Adenine is thus suitable for prelabelling the adenine nucleotide pool. [14C]Guanine and [14C]hypoxanthine were rapidly catabolized to allantoin, whereas nucleotide synthesis was low. [14C]Adenosine was initially phosphorylated and deaminated at about equal rates, but with continued incubation catabolic products predominated. Isolated hepatocytes were found suitable for studies of purine metabolism, in which the liver has important functions for the whole organism.

摘要

通过胶原酶灌注制备大鼠肝细胞悬液,研究了腺嘌呤、次黄嘌呤、鸟嘌呤和腺苷的代谢。根据用[14C]腺嘌呤孵育后ATP中放射性与ADP中放射性的比率判断,氧气供应是细胞制备及后续孵育中的关键变量。该比率被建议作为细胞功能的额外标准。由[14C]腺嘌呤合成的腺嘌呤核苷酸缓慢分解代谢为尿囊素,很少有放射性掺入其他嘌呤化合物。因此,[14C]腺嘌呤适用于对腺嘌呤核苷酸池进行预标记。[14C]鸟嘌呤和[14C]次黄嘌呤迅速分解代谢为尿囊素,而核苷酸合成较低。[14C]腺苷最初磷酸化和脱氨的速率大致相等,但随着孵育的持续,分解代谢产物占主导。发现分离的肝细胞适用于嘌呤代谢研究,其中肝脏对整个机体具有重要功能。

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引用本文的文献

1
Purine catabolism in isolated rat hepatocytes. Influence of coformycin.离体大鼠肝细胞中的嘌呤分解代谢。助间霉素的影响。
Biochem J. 1980 Jun 15;188(3):913-20. doi: 10.1042/bj1880913.
2
Uptake and utilization of 5'-methylthioadenosine by cultured baby-hamster kidney cells.培养的幼仓鼠肾细胞对5'-甲硫腺苷的摄取与利用
Biochem J. 1982 Jun 15;204(3):803-7. doi: 10.1042/bj2040803.
3
Metabolism of hypoxanthine in isolated rat hepatocytes.次黄嘌呤在离体大鼠肝细胞中的代谢
Biochem J. 1984 Aug 15;222(1):145-55. doi: 10.1042/bj2220145.