1985
DOI: 10.1111/j.1432-1033.1985.tb08810.x
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Purification of GTP:α‐d‐mannose‐1‐phosphate guanyltransferase

Abstract: The enzyme GTP:α‐d‐mannose‐1‐phosphate guanylyltransferase from porcine thyroid tissue has been purified 69 900‐fold on columns of blue‐Sepharose, DEAE‐Sepharose, phenyl‐Sepharose and agarose‐GTP affinity materials. Although it exhibits a tendency to aggregate, the enzyme travelled, upon sucrose velocity sedimentation, as a single oligomer with a molecular mass of 412 kDa. Michaelis constants were determined to be 1.0 μM, 1.0 mM, 3.5 μM and 0.4 μM for GDP‐α‐d‐mannose, pyrophosphate, GTP and mannose‐1‐phosphate… Show more

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Cited by 9 publications
(1 citation statement)
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“…GDP- d -mannose pyrophosphorylase (EC 2.7.7.13, d -mannose-1-phosphate guanylyltransferase, GMPase) catalyzes the conversion of d -mannose-1-P to GDP- d -mannose in mammals, plants, yeasts and bacteria [1]. In plants, GDP- d -mannose is used to synthesize not only structural carbohydrates but also ascorbic acid (AsA) [24].…”
Section: Introductionmentioning
confidence: 99%
“…GDP- d -mannose pyrophosphorylase (EC 2.7.7.13, d -mannose-1-phosphate guanylyltransferase, GMPase) catalyzes the conversion of d -mannose-1-P to GDP- d -mannose in mammals, plants, yeasts and bacteria [1]. In plants, GDP- d -mannose is used to synthesize not only structural carbohydrates but also ascorbic acid (AsA) [24].…”
Section: Introductionmentioning
confidence: 99%