A Multifunctional Protein Possessing Glycinamide Ribonucleotide Synthetase, Glycinamide Ribonucleotide Transformylase, and Aminoimidazole Ribonucleotide Synthetase Activities in de Novo Purine Biosynthesis

Susan Colette Daubner, Jo Ann Stubbe, Stephen Benkovic, Jeffrey L. Schrimsher, Frederick J. Schendel, Mark Young, Steven Henikoff, David Patterson

Research output: Contribution to journalArticle

48 Citations (Scopus)

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 110000. 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.

Original languageEnglish (US)
Pages (from-to)7059-7062
Number of pages4
JournalBiochemistry
Volume24
Issue number25
DOIs
StatePublished - Dec 1 1985

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Phosphoribosylglycinamide Formyltransferase
Ribonucleotides
Biosynthesis
Ligases
Sodium Dodecyl Sulfate
Proteolysis
Chickens
Proteins
Molecular Weight
Western Blotting
Gels
Liver
Peptides
Purification
Antibodies
Precipitates
Resins
Molecular weight
purine
phosphoribosylamine-glycine ligase

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Daubner, Susan Colette ; Stubbe, Jo Ann ; Benkovic, Stephen ; Schrimsher, Jeffrey L. ; Schendel, Frederick J. ; Young, Mark ; Henikoff, Steven ; Patterson, David. / A Multifunctional Protein Possessing Glycinamide Ribonucleotide Synthetase, Glycinamide Ribonucleotide Transformylase, and Aminoimidazole Ribonucleotide Synthetase Activities in de Novo Purine Biosynthesis. In: Biochemistry. 1985 ; Vol. 24, No. 25. pp. 7059-7062.
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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 110000. 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.",
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A Multifunctional Protein Possessing Glycinamide Ribonucleotide Synthetase, Glycinamide Ribonucleotide Transformylase, and Aminoimidazole Ribonucleotide Synthetase Activities in de Novo Purine Biosynthesis. / Daubner, Susan Colette; Stubbe, Jo Ann; Benkovic, Stephen; Schrimsher, Jeffrey L.; Schendel, Frederick J.; Young, Mark; Henikoff, Steven; Patterson, David.

In: Biochemistry, Vol. 24, No. 25, 01.12.1985, p. 7059-7062.

Research output: Contribution to journalArticle

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AU - Daubner, Susan Colette

AU - Stubbe, Jo Ann

AU - Benkovic, Stephen

AU - Schrimsher, Jeffrey L.

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AU - Henikoff, Steven

AU - Patterson, David

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AB - 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 110000. 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.

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