Enzymatic assay procedures that employ high-performance liquid chromatography: Competition between phosphoribosyltransferases for a common substrate

Donald L. Sloan, Linda Z. Ali, Diogenese Aybar-Batista, Cong Yan, Susan L. Hess

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

A survey of the phosphoribosyltransferase (PRTase) activities in yeast has been accomplished using reversed-phase high-performance liquid chromatographic assay procedures. The following bases were observed to be utilized during phosphoribosyl pyrophosphate (PRibPP)-dependent nucleotide syntheses: adenine, xanthine, hypoxanthine, guanine, uracil, orotate, nicotinamide, nicotinate and quinolinate. Gradient elution procedures have also been perfected that allow the separation of the two following sets of PRTase assay components: (1) adenosine monophosphate, nicotinate mononucleotide, orotate, adenosine triphosphate, nicotinate, adenosine diphosphate, inosine monophosphate and hypoxanthine, and (2) nicotinate mononucleotide, nicotinamide mononucleotide, adenosine triphosphate, nicotinate, adenosine diphosphate and nicotinamide. Separation 1 has been employed to examine the PRibPP allocation among the hypoxanthine PRTase, orotate PRTase and nicotinate PRTase catalyzed reactions, whereas separation 2 has been employed to define the role that ATP plays in the nicotinamide PRTase-catalyzed reaction along with the allocation of nicotinamide between the reactions catalysed by nicotinamide PRTase and nicotinamide deamidase.

Original languageEnglish (US)
Pages (from-to)43-52
Number of pages10
JournalJournal of Chromatography A
Volume316
Issue numberC
DOIs
StatePublished - 1984
Externally publishedYes

Fingerprint

Niacinamide
Niacin
Enzyme Assays
High performance liquid chromatography
Phosphoribosyl Pyrophosphate
Nicotinamide Phosphoribosyltransferase
Assays
Hypoxanthine
Adenosine Triphosphate
High Pressure Liquid Chromatography
Adenosine Diphosphate
Nicotinamidase
Nicotinamide Mononucleotide
Orotate Phosphoribosyltransferase
Substrates
Quinolinic Acid
Hypoxanthine Phosphoribosyltransferase
Inosine Monophosphate
Xanthine
Uracil

ASJC Scopus subject areas

  • Analytical Chemistry
  • Clinical Biochemistry
  • Molecular Medicine

Cite this

Enzymatic assay procedures that employ high-performance liquid chromatography : Competition between phosphoribosyltransferases for a common substrate. / Sloan, Donald L.; Ali, Linda Z.; Aybar-Batista, Diogenese; Yan, Cong; Hess, Susan L.

In: Journal of Chromatography A, Vol. 316, No. C, 1984, p. 43-52.

Research output: Contribution to journalArticle

@article{1c48d9f0646f4d86b7614d825526d7f6,
title = "Enzymatic assay procedures that employ high-performance liquid chromatography: Competition between phosphoribosyltransferases for a common substrate",
abstract = "A survey of the phosphoribosyltransferase (PRTase) activities in yeast has been accomplished using reversed-phase high-performance liquid chromatographic assay procedures. The following bases were observed to be utilized during phosphoribosyl pyrophosphate (PRibPP)-dependent nucleotide syntheses: adenine, xanthine, hypoxanthine, guanine, uracil, orotate, nicotinamide, nicotinate and quinolinate. Gradient elution procedures have also been perfected that allow the separation of the two following sets of PRTase assay components: (1) adenosine monophosphate, nicotinate mononucleotide, orotate, adenosine triphosphate, nicotinate, adenosine diphosphate, inosine monophosphate and hypoxanthine, and (2) nicotinate mononucleotide, nicotinamide mononucleotide, adenosine triphosphate, nicotinate, adenosine diphosphate and nicotinamide. Separation 1 has been employed to examine the PRibPP allocation among the hypoxanthine PRTase, orotate PRTase and nicotinate PRTase catalyzed reactions, whereas separation 2 has been employed to define the role that ATP plays in the nicotinamide PRTase-catalyzed reaction along with the allocation of nicotinamide between the reactions catalysed by nicotinamide PRTase and nicotinamide deamidase.",
author = "Sloan, {Donald L.} and Ali, {Linda Z.} and Diogenese Aybar-Batista and Cong Yan and Hess, {Susan L.}",
year = "1984",
doi = "10.1016/S0021-9673(00)96139-9",
language = "English (US)",
volume = "316",
pages = "43--52",
journal = "Journal of Chromatography",
issn = "0021-9673",
publisher = "Elsevier",
number = "C",

}

TY - JOUR

T1 - Enzymatic assay procedures that employ high-performance liquid chromatography

T2 - Competition between phosphoribosyltransferases for a common substrate

AU - Sloan, Donald L.

AU - Ali, Linda Z.

AU - Aybar-Batista, Diogenese

AU - Yan, Cong

AU - Hess, Susan L.

PY - 1984

Y1 - 1984

N2 - A survey of the phosphoribosyltransferase (PRTase) activities in yeast has been accomplished using reversed-phase high-performance liquid chromatographic assay procedures. The following bases were observed to be utilized during phosphoribosyl pyrophosphate (PRibPP)-dependent nucleotide syntheses: adenine, xanthine, hypoxanthine, guanine, uracil, orotate, nicotinamide, nicotinate and quinolinate. Gradient elution procedures have also been perfected that allow the separation of the two following sets of PRTase assay components: (1) adenosine monophosphate, nicotinate mononucleotide, orotate, adenosine triphosphate, nicotinate, adenosine diphosphate, inosine monophosphate and hypoxanthine, and (2) nicotinate mononucleotide, nicotinamide mononucleotide, adenosine triphosphate, nicotinate, adenosine diphosphate and nicotinamide. Separation 1 has been employed to examine the PRibPP allocation among the hypoxanthine PRTase, orotate PRTase and nicotinate PRTase catalyzed reactions, whereas separation 2 has been employed to define the role that ATP plays in the nicotinamide PRTase-catalyzed reaction along with the allocation of nicotinamide between the reactions catalysed by nicotinamide PRTase and nicotinamide deamidase.

AB - A survey of the phosphoribosyltransferase (PRTase) activities in yeast has been accomplished using reversed-phase high-performance liquid chromatographic assay procedures. The following bases were observed to be utilized during phosphoribosyl pyrophosphate (PRibPP)-dependent nucleotide syntheses: adenine, xanthine, hypoxanthine, guanine, uracil, orotate, nicotinamide, nicotinate and quinolinate. Gradient elution procedures have also been perfected that allow the separation of the two following sets of PRTase assay components: (1) adenosine monophosphate, nicotinate mononucleotide, orotate, adenosine triphosphate, nicotinate, adenosine diphosphate, inosine monophosphate and hypoxanthine, and (2) nicotinate mononucleotide, nicotinamide mononucleotide, adenosine triphosphate, nicotinate, adenosine diphosphate and nicotinamide. Separation 1 has been employed to examine the PRibPP allocation among the hypoxanthine PRTase, orotate PRTase and nicotinate PRTase catalyzed reactions, whereas separation 2 has been employed to define the role that ATP plays in the nicotinamide PRTase-catalyzed reaction along with the allocation of nicotinamide between the reactions catalysed by nicotinamide PRTase and nicotinamide deamidase.

UR - http://www.scopus.com/inward/record.url?scp=0021647706&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021647706&partnerID=8YFLogxK

U2 - 10.1016/S0021-9673(00)96139-9

DO - 10.1016/S0021-9673(00)96139-9

M3 - Article

C2 - 6241619

AN - SCOPUS:0021647706

VL - 316

SP - 43

EP - 52

JO - Journal of Chromatography

JF - Journal of Chromatography

SN - 0021-9673

IS - C

ER -