EurekaMag.com logo
+ Site Statistics
References:
53,214,146
Abstracts:
29,074,682
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Preparation of iodine 125 catalytic subunit of aspartate trans carbamylase and its use in studies of the regulatory subunit


Journal of Biological Chemistry 248(11): 3762-3768
Preparation of iodine 125 catalytic subunit of aspartate trans carbamylase and its use in studies of the regulatory subunit

(PDF 0-2 workdays service: $29.90)

Accession: 006173338



Related references

Subunit interactions in aspartate trans carbamylase ec 2.1.3.2 characterization of a complex between the catalytic and the regulatory subunits. Journal of Biological Chemistry 250(2): 653-660, 1975

Subunit interactions in aspartate trans carbamylase ec 2.1.3.2 the interaction between catalytic and regulatory subunits and the effect of ligands. Journal of Biological Chemistry 250(2): 661-667, 1975

Binding of regulatory nucleotides to aspartate trans carbamylase ec 2.1.3.2 nmr studies of selectively enriched carbon 13 regulatory subunit. Biochemistry 19(25): 5768-5773, 1980

Medium resolution hydrogen exchange studies of the catalytic subunit c 3 of escherichia coli aspartate trans carbamylase. Biophysical Journal 37(2 PART 2): 6A, 1982

Aspartate trans carbamylase a nmr study of the binding of inhibitors and substrates to the catalytic subunit. Journal of Biological Chemistry 244(7): 1860-1808, 1969

Inactivation of the catalytic subunit of aspartate trans carbamylase ec 2.1.3.2 by nitration with tetra nitro methane. Journal of Biological Chemistry 255(2): 602-607, 1980

Aspartate trans carbamylase a study by transient nmr of the binding of succinate to the native enzyme and its catalytic subunit. Journal of Biological Chemistry 245(5): 1180-1189, 1970

Binding of succinate to aspartate trans carbamylase catalytic subunit ph and temperature dependence of nmr relaxation times. Biochemistry 12(12): 2255-2264, 1973

Energetics of the binding of substrates and substrate analogs to escherichia coli aspartate trans carbamylase and its catalytic subunit. Biophysical Journal 17(2): 181A, 1977

Response to the adenylate energy charge by escherichia coli enz aspartate trans carbamylase and its catalytic subunit abstract. Federation Proceedings 28(2): 341, 1969