支原体感染的骨髓瘤细胞中存在一种新的鸟氨酸转甲氨基酶。

Enzyme & protein Pub Date : 1993-01-01 DOI:10.1159/000468658
F Matsuno, H Matsuzaki, Y Akahoshi, M Yoshida, H Hata, M Takiguchi, K Takatsuki, M Mori
{"title":"支原体感染的骨髓瘤细胞中存在一种新的鸟氨酸转甲氨基酶。","authors":"F Matsuno,&nbsp;H Matsuzaki,&nbsp;Y Akahoshi,&nbsp;M Yoshida,&nbsp;H Hata,&nbsp;M Takiguchi,&nbsp;K Takatsuki,&nbsp;M Mori","doi":"10.1159/000468658","DOIUrl":null,"url":null,"abstract":"<p><p>A myeloma cell line (KHM-4) from a patient with multiple myeloma and idiopathic hyperammonemia, and another myeloma cell line (RPMI8226) were seen to have activity to form ammonia from arginine. High activity of ornithine transcarbamylase (OTC), a hepatic urea cycle enzyme, was detected in these cell lines. OTC of these cells was much more heat-stable than the liver enzyme, and did not cross-react with an antibody against the liver enzyme. As the OTC activity was also detected in the culture medium of the myeloma cells and because the activity was markedly decreased by the antimycoplasma drug MC-210, the OTC activity was assumed to be associated with mycoplasma infection. Polymerase chain reaction, using degenerate oligonucleotide mixtures corresponding to the two highly conserved sequences of OTC, amplified a DNA sequence that apparently encodes a portion (about 67% in length) of mycoplasma OTC. The predicted amino acid sequence of the mycoplasma enzyme was 33-47% identical with those of the enzymes of bacteria, yeast and mammals.</p>","PeriodicalId":11854,"journal":{"name":"Enzyme & protein","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1993-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000468658","citationCount":"4","resultStr":"{\"title\":\"A novel ornithine transcarbamylase present in mycoplasma-infected myeloma cells.\",\"authors\":\"F Matsuno,&nbsp;H Matsuzaki,&nbsp;Y Akahoshi,&nbsp;M Yoshida,&nbsp;H Hata,&nbsp;M Takiguchi,&nbsp;K Takatsuki,&nbsp;M Mori\",\"doi\":\"10.1159/000468658\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A myeloma cell line (KHM-4) from a patient with multiple myeloma and idiopathic hyperammonemia, and another myeloma cell line (RPMI8226) were seen to have activity to form ammonia from arginine. High activity of ornithine transcarbamylase (OTC), a hepatic urea cycle enzyme, was detected in these cell lines. OTC of these cells was much more heat-stable than the liver enzyme, and did not cross-react with an antibody against the liver enzyme. As the OTC activity was also detected in the culture medium of the myeloma cells and because the activity was markedly decreased by the antimycoplasma drug MC-210, the OTC activity was assumed to be associated with mycoplasma infection. Polymerase chain reaction, using degenerate oligonucleotide mixtures corresponding to the two highly conserved sequences of OTC, amplified a DNA sequence that apparently encodes a portion (about 67% in length) of mycoplasma OTC. The predicted amino acid sequence of the mycoplasma enzyme was 33-47% identical with those of the enzymes of bacteria, yeast and mammals.</p>\",\"PeriodicalId\":11854,\"journal\":{\"name\":\"Enzyme & protein\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1993-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1159/000468658\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Enzyme & protein\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1159/000468658\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Enzyme & protein","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000468658","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 4

摘要

来自多发性骨髓瘤和特发性高氨血症患者的骨髓瘤细胞系(KHM-4)和另一个骨髓瘤细胞系(RPMI8226)被发现具有从精氨酸生成氨的活性。在这些细胞系中检测到高活性的鸟氨酸转氨基甲酰基酶(OTC),一种肝脏尿素循环酶。这些细胞的OTC比肝酶更热稳定,并且不会与针对肝酶的抗体发生交叉反应。由于在骨髓瘤细胞培养基中也检测到OTC活性,并且由于抗支原体药物MC-210显著降低了OTC活性,因此认为OTC活性与支原体感染有关。聚合酶链反应,利用与支原体OTC的两个高度保守序列相对应的简并寡核苷酸混合物,扩增出一个DNA序列,该序列显然编码了支原体OTC的一部分(长度约67%)。预测的支原体酶的氨基酸序列与细菌、酵母和哺乳动物酶的氨基酸序列吻合度为33 ~ 47%。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
A novel ornithine transcarbamylase present in mycoplasma-infected myeloma cells.

A myeloma cell line (KHM-4) from a patient with multiple myeloma and idiopathic hyperammonemia, and another myeloma cell line (RPMI8226) were seen to have activity to form ammonia from arginine. High activity of ornithine transcarbamylase (OTC), a hepatic urea cycle enzyme, was detected in these cell lines. OTC of these cells was much more heat-stable than the liver enzyme, and did not cross-react with an antibody against the liver enzyme. As the OTC activity was also detected in the culture medium of the myeloma cells and because the activity was markedly decreased by the antimycoplasma drug MC-210, the OTC activity was assumed to be associated with mycoplasma infection. Polymerase chain reaction, using degenerate oligonucleotide mixtures corresponding to the two highly conserved sequences of OTC, amplified a DNA sequence that apparently encodes a portion (about 67% in length) of mycoplasma OTC. The predicted amino acid sequence of the mycoplasma enzyme was 33-47% identical with those of the enzymes of bacteria, yeast and mammals.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信