Polyprenol phosphates and mannosyl transferases in Phaseolus aureus

Alam, Syed Sartaj; Hemming, Frank W.

doi:10.1016/0031-9422(73)80382-6

Cited by 32 publications

(13 citation statements)

References 17 publications

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“…The transferases are associated with cell particulate fractions and are thus similar to those previously described in animal systems (14) and other plant systems (1,5,7). The lipid-linked fractions formed from GDPmannose appear to be lipid monosaccharide soluble in chloroform-methanol (2:1) and a lipid-linked oligosaccharide soluble in chloroform-methanol-water (1:1:0.3).…”

Section: Resultssupporting

confidence: 60%

“…This oligosaccharidelipid serves as the carrier of the oligosaccharide chain which combines with the polypeptide to produce glycoproteins (14,17). Similar lipid intermediates have been implicated in the biosynthesis of glycoproteins in shoots of mung bean seedlings (1,7,11), cotton fibers (6), and cotyledons of Phaseolus vulgaris (5).As part of our continuing studies of protein synthesis in the Beckman L2-65B centrifuge. The supernatant from this centrifugation was discarded and the surface of the remaining pellet was washed with reaction medium.…”

mentioning

confidence: 99%

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Glycoprotein Biosynthesis in Cotyledons of Pisum sativum L

Beevers¹,

Mense²

1977

Plant Physiol.

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The reserve globulins, legumin and vicilin, in the pea cotyledon are glycoproteins. Acid hydrolysis of these glycoproteins releases the amino-sugar glucosamine and neutral sugars, principally mannose (2). Similar glycosyl components occur in the glycoproteins from animal tissues (16,27). Studies with extracts from animal tissues have established that the glycosyl components in the glycoproteins are derived originally from nucleotide sugars. The glycosyl components from the nucleotide sugars are transferred to lipid (polyisoprenol) intermediates to form lipidlinked monosaccharides which serve as precursors for the formation of lipid-linked oligosaccharides. This oligosaccharidelipid serves as the carrier of the oligosaccharide chain which combines with the polypeptide to produce glycoproteins (14,17). Similar lipid intermediates have been implicated in the biosynthesis of glycoproteins in shoots of mung bean seedlings (1,7,11), cotton fibers (6), and cotyledons of Phaseolus vulgaris (5).As part of our continuing studies of protein synthesis in the Beckman L2-65B centrifuge. The supernatant from this centrifugation was discarded and the surface of the remaining pellet was washed with reaction medium. Pellets were suspended in 3 ml of reaction mixture which, unless stated otherwise, consisted of 50 mm tris-HCl (pH 7) containing 10 mm KCI, 10 mm MgCI2, and 5 mm 2-mercaptoethanol. This suspension of cellular particulates was used as the enzyme source. Corporation). After a 60-min incubation at 37 C the reaction was terminated by the addition of 0.7 ml of H20 and 2.5 ml of chloroform-methanol (2:1, v/v). After thorough mixing the phases were separated by centrifugation and the lower organic phase recovered. The upper aqueous layer and interphase were reextracted with 2.5 ml of 2:1 chloroform-methanol; the organic phase was collected and pooled with the previous extraction.These pooled 2:1 chloroform-methanol fractions were then washed twice with 2.5 ml of chloroform-methanol-water (3:48:47). At each extraction the upper phase was discarded.The recovered washed 2:1 chloroform-methanol fraction was placed in a scintillation vial, evaporated to dryness, and radioactivity determined upon the addition of scintillation fluid (8 g 2,5-diphenyloxazole [PPOt in 2 liters of toluene, 1 liter of Triton X-100).The aqueous phase and interphase remaining after chloro-

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Section: Resultssupporting

confidence: 60%

mentioning

confidence: 99%

Glycoprotein Biosynthesis in Cotyledons of Pisum sativum L

Beevers¹,

Mense²

1977

Plant Physiol.

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“…In higher plants, particulate mannosyltransferases have been reported in Phaseolus aureus (1,13,16,18,26) and cotton fibers (8,9). Recently also, N-acetylglucosaminyl transferase activity has been reported in mung bean hypototyls (24) and cotton fibers (9).…”

Section: Discussionmentioning

confidence: 99%

“…The occurrence of polyprenol-linked sugars in plants has been studied intensively in recent years (1,8,9,13,16,18). However, the role of polyprenol-linked sugars as intermediates for the transfer of sugars to glycans is not as well understood for plants as it is for animals and bacteria (2,13,18).…”

mentioning

confidence: 99%

Membrane-bound UDP-Glucose

Lezica¹,

Romero²,

Dankert³

1976

Plant Physiol.

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An enzymic preparation from peas (Pisum satisum), able to fonn netral ad polar glycosides, is described. The best sugar donor is UDPglucose ad the acceptors are present in the enzymic system. of the neutral glucolipid-synthesizing activity, and the fraction that sediments at 100,000g is rich in polar glucolipid glucosyl transferase activity. This latter activity was strongly dependent on Mg+ concentration, the optimum being around 5 to 10 mM. UDP inhibits the reaction and 0.2 to 0.5% (v/v) Triton X-100 has a stimulatory effect. The optimum pH is 7.5.

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“…It has been detected in mammalian tissues [2], plants [3][4][5], insects [6], yeast [7,8] and other eucaryotic cells [1 ]. The biosynthesis of dolichyl phosphate may be envisaged to occur either by dephosphorylation of the pyrophosphate derivative (presumably formed from lower molecular weight precursors [9][10][11][12]) or by phosphorylation of free dolichol which is generally found in considerable amounts as compared with its phosphate [13].…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of dolichol by insect enzymes

Allué¹

1979

FEBS Letters

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Polyprenol phosphates and mannosyl transferases in Phaseolus aureus

Cited by 32 publications

References 17 publications

Glycoprotein Biosynthesis in Cotyledons of Pisum sativum L

Glycoprotein Biosynthesis in Cotyledons of Pisum sativum L

Membrane-bound UDP-Glucose

Phosphorylation of dolichol by insect enzymes

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