1973
DOI: 10.1042/bj1350125
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Enzyme forms produced from aspartate transcarbamoylase by digestion with trypsin

Abstract: 1. The time-course of tryptic hydrolysis of aspartate transcarbamoylase (aspartate carbamoyltransferase, EC 2.1.3.2) was followed by activity measurements in the presence and absence of allosteric effectors, and by polyacrylamide-gel electrophoresis. 2. Two proteins with enzyme activity are formed in this way from native enzyme, and the isolation and some properties of these species are reported. The larger protein (10.6S) resembles native enzyme in that it contains regulatory subunits and is sensitive to allo… Show more

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Cited by 11 publications
(1 citation statement)
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“…Moreover, we would expect RNRNRs(C)2 and r4c6 to differ significantly since the former would have a shielded cavity and the latter would permit access through an entire side of the molecule. No (29). Although the composition of this component has not been established, it should be noted that it is similar to r4c,5 in sedimentation coefficient, in electrophoretic mobility on polyacrylamide gels, and in kinetic behavior.…”
mentioning
confidence: 99%
“…Moreover, we would expect RNRNRs(C)2 and r4c6 to differ significantly since the former would have a shielded cavity and the latter would permit access through an entire side of the molecule. No (29). Although the composition of this component has not been established, it should be noted that it is similar to r4c,5 in sedimentation coefficient, in electrophoretic mobility on polyacrylamide gels, and in kinetic behavior.…”
mentioning
confidence: 99%