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  • 标题:Stopped-flow x-ray scattering: the dissociation of aspartate transcarbamylase
  • 本地全文:下载
  • 作者:M F Moody ; P Vachette ; A M Foote
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1980
  • 卷号:77
  • 期号:7
  • 页码:4040-4043
  • DOI:10.1073/pnas.77.7.4040
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:A combination of stopped-flow and x-ray scattering techniques was used to study the dissociation of aspartate transcarbamylase (carbamoylphosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2 ) with a 2:1 excess of p-chloromercuribenzenesulfonic acid (the ratio being calculated on a basis of reactive sites), in the presence and absence of the transition state analogue N-(phosphonacetyl)-L-aspartate. At 10 mg of protein per ml, the scattering curves allowed some details of the reaction to be followed with a time resolution down to 1 sec. The curves showed not only the dissociation of the enzyme complex but also the formation of the subunits. These results show that, with present facilities, x-ray scattering could be used to study dissociation or reassociation reactions with a time resolution of the order of 100 msec.
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