PURIFICATION OF ASPARTATE TRANSCARBAMOYLASE FROM PSEUDOMONAS-SYRINGAE

被引：0
作者：
SHEPHERDSON, M
MCPHAIL, D
机构：
来源：
FEMS MICROBIOLOGY LETTERS | 1993年 / 114卷 / 02期
关键词：
ASPARTATE TRANSCARBAMOYLASE; PROTEIN EVOLUTION; PSEUDOMONAS-SYRINGAE;
D O I：
暂无
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
The aspartate transcarbamoylase (ATCase) from Pseudomonas syringae has been purified. The purified enzyme was shown by SDS-PAGE to give two bands. Unambiguous results from N-terminal sequencing suggested that each band represented a homogeneous polypeptide. The M(r) (relative molecular mass) of the polypeptides was estimated to be 47 kDa and 34 kDa. The M(r) of the holoenzyme determined by gel filtration and electrophoretic migration in polyacrylamide gradient gels under non-denaturing conditions was estimated at approximately 490 kDa. These findings suggest a subunit structure different from any previously described for a bacterial ATCase.
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页码：201 / 206
页数：6
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