Abstract：
:Three activities on the pathway of purine biosynthesis de novo in chicken liver, namely, glycinamide ribonucleotide synthetase, glycinamide ribonucleotide transformylase, and aminoimidazole ribonucleotide synthetase, have been found to reside on the same polypeptide chain. Three diverse purification schemes, utilizing three different affinity resins, give rise to the same protein since the final material has identical specific activities for all three enzymatic reactions and a molecular weight on sodium dodecyl sulfate gels of about 110 000. A single antibody preparation precipitates all three activities and binds to the multifunctional protein obtained by two methods in Western blots. Partial chymotryptic digestion of the purified protein gives rise to two fragments, one possessing glycinamide ribonucleotide synthetase activity and the other containing glycinamide ribonucleotide transformylase activity.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Daubner SC,Schrimsher JL,Schendel FJ,Young M,Henikoff S,Patterson D,Stubbe J,Benkovic SJdoi
10.1021/bi00346a006subject
Has Abstractpub_date
1985-12-03 00:00:00pages
7059-62issue
25eissn
0006-2960issn
1520-4995journal_volume
24pub_type
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