Characterization of products synthesized by galactosyltransferase purified from the ascites of ovarian cancer patients.

Characterization of products synthesized by galactosyltransferase purified from the ascites of ovarian cancer patients. Research Abstract Details 

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Characterization of products synthesized by galactosyltransferase purified from the ascites of ovarian cancer patients. Abstract Text:

S K Chatterjee,M Bhattacharya,J J Barlow,

Galactosyltransferase purified from the ascites of ovarian cancer patients can use to an equal extent N-glycosidic glycoproteins, such as asialoagalactofetuin, and O-glycosidic mucin, such as asialo bovine submaxillary mucin (BSM), as acceptors. Thermal treatment and substrate competition experiments demonstrated that the same enzyme catalyzed the transfer of galactose to both types of acceptors. Alkaline borohydride treatment showed that, while the product with asialoagalactofetuin was totally resistant, about 90% of the product with asialo BSM was hydrolyzed by this treatment. Gel filtration of the released oligosaccharides on a calibrated Biogel P-2 column showed three peaks. One major oligosaccharide (O-2) of size 5.7 glucose U and two minor peaks (O-1 and O-3) of sizes 8.7 and 3.7 glucose U, respectively, were obtained. The oligosaccharides were doubly labeled, first by incubation with uridine-diphosphate [14C]galactose, followed by alkali treatment in the presence of [3H]borohydride. The doubly labeled oligosaccharides were separately purified by gel filtration and ion-exchange chromatography and digested with various exoglycosidases. The digested products were characterized by gel filtration and paper chromatography in three different systems. From these results, the structures of these oligosaccharides were computed as follows: O-1 = beta-galactosyl-beta-N-acetylglucosamine-galactosaminitol (sialic acid); O-2 = beta-galactose-beta-N-acetylglucosamine-galactosaminitol; O-3 = beta-galactose-galactosaminitol. These results suggest that the galactosyltransferase from the ascites of ovarian cancer patients catalyzes the transfer of galactose to N-acetylglucosamine, irrespective of whether it is a part of an N-glycan or an O-glycan.

Characterization of products synthesized by galactosyltransferase purified from the ascites of ovarian cancer patients. Publishing Authors By Initials

SK Chatterjee,M Bhattacharya,JJ Barlow,

For similar proteins: fetal proteins: alpha-fetoproteins research abstracts see: proteins: fetal proteins: alpha-fetoproteins research

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Characterization of products synthesized by galactosyltransferase purified from the ascites of ovarian cancer patients. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of the National Cancer Institute

VOLUME: 77

Page Numbers: 855-62

Journal Abbreviation: J. Natl. Cancer Inst.

ISSN: 0027-8874

DAY: 1

MONTH: Oct

YEAR: 1986

Characterization of products synthesized by galactosyltransferase purified from the ascites of ovarian cancer patients. Information

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LANGUAGE: eng

NlmUniqueID: 7503089

Characterization of products synthesized by galactosyltransferase purified from the ascites of ovarian cancer patients. Keywords Mesh Terms:

KEYWORDS: alpha-Fetoproteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Characterization of products synthesized by galactosyltransferase purified from the ascites of ovarian cancer patients. Information

Substance Name: Glycoside Hydrolases

Registry Number: EC 3.2.1.-

Grant and Affiliation Information for Characterization of products synthesized by galactosyltransferase purified from the ascites of ovarian cancer patients.

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Country: UNITED STATES

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MEDLINETA: J Natl Cancer Inst

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