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.
