1967
DOI: 10.1021/bi00864a017
|View full text |Cite
|
Sign up to set email alerts
|

Aspartate Transcarbamylase. Amino-Terminal Analyses and Peptide Maps of the Subunits*

Abstract: suggests that there are four each of the two different kinds of peptide chains in the native enzyme (molecular weight 3.1 X 10s). Taken together with the data of Changeux et al. (Changeux, J.-P., Gerhart, J. C., and Schachman, . K. (1967), in Regulation of Nucleic Acid and Protein Biosynthesis, Koningsberger, V. V., and Bosch, L, Ed., New York, N. Y., Elsevier, p 344) our results indicate that each of the binding sites for succinate (a competitive inhibitor of aspartatate) and cytidine triphosphate resides on … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

1970
1970
1994
1994

Publication Types

Select...
3
2
1

Relationship

0
6

Authors

Journals

citations
Cited by 22 publications
(1 citation statement)
references
References 14 publications
(15 reference statements)
0
1
0
Order By: Relevance
“…Independent confirmation of the tetramer configuration was obtained by other investigators [99,100] through methods of MW determination in urea, amino-terminal residues, and peptide analysis. However, a further probing by Weber [101], through subunit determination after denaturation with sodium dodecylsulfate, analysis of carboxy-terminal residues, and a proposed amino acid sequence for the R chain, has led to a rejection of the tetramer model in favor of a hexamer.…”
Section: Aspartate Transcarbamylase (Ec 2132)mentioning
confidence: 82%
“…Independent confirmation of the tetramer configuration was obtained by other investigators [99,100] through methods of MW determination in urea, amino-terminal residues, and peptide analysis. However, a further probing by Weber [101], through subunit determination after denaturation with sodium dodecylsulfate, analysis of carboxy-terminal residues, and a proposed amino acid sequence for the R chain, has led to a rejection of the tetramer model in favor of a hexamer.…”
Section: Aspartate Transcarbamylase (Ec 2132)mentioning
confidence: 82%