UDP-N-Acetyl-D-glucosamine-Asparagine sequon N-Acetyl-β-D-Glucosaminyl -Transferase-Activity in Human serum

Zhila Khalkhali; R. Derek Marshall

doi:10.1016/S0008-6215(00)83163-8

UDP-N-Acetyl-D-glucosamine-Asparagine sequon N-Acetyl-β-D-Glucosaminyl -Transferase-Activity in Human serum

Zhila Khalkhali^*, R. Derek Marshall

^*Corresponding author for this work

Pediatrics

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

Serum contains a sugar transferase which is able to catalyse the glycosylation in in vitro of the asparagine residue present in the sequence Asn.Leu.Thr in bovine pancreatic ribonuclease. UDP-2-Acetamido-2-deoxy-D-glucose (UDP-N-acetyl-D- glucosamine) acts as the donor, although the mechanism of the transfer is unexplored. Spermidine and Mn²⁺, as well as CDP-choline, can act as activators for the reaction. Monoglycosylated ribonuclease (ribonuclease-GIcNAc) has been separated (23% yield) from unreacted ribonuclease A by affinity chromatography on a colunm of wheat-germ agglutinin bound to Sepharose, and characterised. A possible reason for the presence of the enzyme in serum is suggested.

Original language	English (US)
Pages (from-to)	455-473
Number of pages	19
Journal	Carbohydrate Research
Volume	49
Issue number	C
DOIs	https://doi.org/10.1016/S0008-6215(00)83163-8
State	Published - Jul 1976

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry
Organic Chemistry

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@article{14aa8802d28f4166813ff958d62fca0e,

title = "UDP-N-Acetyl-D-glucosamine-Asparagine sequon N-Acetyl-β-D-Glucosaminyl -Transferase-Activity in Human serum",

abstract = "Serum contains a sugar transferase which is able to catalyse the glycosylation in in vitro of the asparagine residue present in the sequence Asn.Leu.Thr in bovine pancreatic ribonuclease. UDP-2-Acetamido-2-deoxy-D-glucose (UDP-N-acetyl-D- glucosamine) acts as the donor, although the mechanism of the transfer is unexplored. Spermidine and Mn2+, as well as CDP-choline, can act as activators for the reaction. Monoglycosylated ribonuclease (ribonuclease-GIcNAc) has been separated (23% yield) from unreacted ribonuclease A by affinity chromatography on a colunm of wheat-germ agglutinin bound to Sepharose, and characterised. A possible reason for the presence of the enzyme in serum is suggested.",

author = "Zhila Khalkhali and Marshall, {R. Derek}",

note = "Funding Information: We thank Dr. Michel Monsigny, Centre de Biophysique Moleculaire, C.N.R.S., Orleans, France, for a gift of wheat-germ agglutinin bound to Sepharose. Ms. Z. Khalkhali is a British Council Scholar on leave of absence from Tehran University Nuclear Centre, Tehran, Iran. The work was supported by funds from the Cancer Research Campaign and by the British Council.",

year = "1976",

month = jul,

doi = "10.1016/S0008-6215(00)83163-8",

language = "English (US)",

volume = "49",

pages = "455--473",

journal = "Carbohydrate Research",

issn = "0008-6215",

publisher = "Elsevier BV",

number = "C",

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T1 - UDP-N-Acetyl-D-glucosamine-Asparagine sequon N-Acetyl-β-D-Glucosaminyl -Transferase-Activity in Human serum

AU - Khalkhali, Zhila

AU - Marshall, R. Derek

N1 - Funding Information: We thank Dr. Michel Monsigny, Centre de Biophysique Moleculaire, C.N.R.S., Orleans, France, for a gift of wheat-germ agglutinin bound to Sepharose. Ms. Z. Khalkhali is a British Council Scholar on leave of absence from Tehran University Nuclear Centre, Tehran, Iran. The work was supported by funds from the Cancer Research Campaign and by the British Council.

PY - 1976/7

Y1 - 1976/7

N2 - Serum contains a sugar transferase which is able to catalyse the glycosylation in in vitro of the asparagine residue present in the sequence Asn.Leu.Thr in bovine pancreatic ribonuclease. UDP-2-Acetamido-2-deoxy-D-glucose (UDP-N-acetyl-D- glucosamine) acts as the donor, although the mechanism of the transfer is unexplored. Spermidine and Mn2+, as well as CDP-choline, can act as activators for the reaction. Monoglycosylated ribonuclease (ribonuclease-GIcNAc) has been separated (23% yield) from unreacted ribonuclease A by affinity chromatography on a colunm of wheat-germ agglutinin bound to Sepharose, and characterised. A possible reason for the presence of the enzyme in serum is suggested.

AB - Serum contains a sugar transferase which is able to catalyse the glycosylation in in vitro of the asparagine residue present in the sequence Asn.Leu.Thr in bovine pancreatic ribonuclease. UDP-2-Acetamido-2-deoxy-D-glucose (UDP-N-acetyl-D- glucosamine) acts as the donor, although the mechanism of the transfer is unexplored. Spermidine and Mn2+, as well as CDP-choline, can act as activators for the reaction. Monoglycosylated ribonuclease (ribonuclease-GIcNAc) has been separated (23% yield) from unreacted ribonuclease A by affinity chromatography on a colunm of wheat-germ agglutinin bound to Sepharose, and characterised. A possible reason for the presence of the enzyme in serum is suggested.

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DO - 10.1016/S0008-6215(00)83163-8

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C2 - 986874

AN - SCOPUS:0016982512

SN - 0008-6215

VL - 49

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EP - 473

JO - Carbohydrate Research

JF - Carbohydrate Research

IS - C

ER -

UDP-N-Acetyl-D-glucosamine-Asparagine sequon N-Acetyl-β-D-Glucosaminyl -Transferase-Activity in Human serum

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