Chemical modification of glycosaminoglycans. Sulphation of heparan sulphate derivatives obtained by periodate oxidation/borohydride reduction

1996 ◽  
Vol 31 (4) ◽  
pp. 211-214 ◽  
Author(s):  
José Kovensky ◽  
Alicia Fernández Cirelli
Keyword(s):  
Chemical Modification ◽  
Heparan Sulphate ◽  
Periodate Oxidation ◽  
Borohydride Reduction

scholarly journals Structural studies on heparan sulphate from human lung fibroblasts. Characterization of oligosaccharides obtained by selective periodate oxidation of d-glucuronic acid residues followed by scission in alkali

1980 ◽  
Vol 191 (1) ◽  
pp. 103-110 ◽  
Author(s):  
Ingrid Sjöberg ◽  
Lars-Ȧke Fransson
Keyword(s):  
Uronic Acid ◽  
Glucuronic Acid ◽  
Human Lung ◽  
General Structure ◽  
Heparan Sulphate ◽  
Periodate Oxidation ◽  
Exchange Chromatography ◽  
Lung Fibroblasts ◽  
Human Lung Fibroblasts ◽  
Iduronic Acid

1. 3H- and 35S-labelled heparan sulphate was isolated from monolayers of human lung fibroblasts and subjected to degradations by (a) deaminative cleavage and (b) periodate oxidation/alkaline elimination. Fragments were resolved by gel- and ion-exchange-chromatography. 2. Deaminative cleavage of the radioactive glycan afforded mainly disaccharides with a low content of ester-sulphate and free sulphate, indicating that a large part (approx. 80%) of the repeating units consisted of uronosyl-glucosamine-N-sulphate. Blocks of non-sulphated [glucuronosyl-N-acetyl glucosamine] repeats (3–4 consecutive units) accounted for the remainder of the chains. 3. By selective oxidation of glucuronic acid residues associated with N-acetylglucosamine, followed by scission in alkali, the radioactive glycan was degraded into a series of fragments. The glucuronosyl-N-acetylglucosamine-containing block regions yielded a compound N-acetylglucosamine–R, where R is the remnant of an oxidized and degraded glucuronic acid. Periodate-insensitive uronic acid residues were recovered in saccharides of the general structure glucosamine–(uronic acid–glucosamine)n–R. 4. Further degradations of these saccharides via deaminative cleavage and re-oxidations with periodate revealed that iduronic acid may be located in sequences such as glucosamine-N-sulphate→iduronic acid→N-acetylglucosamine. Occasionally the iduronic acid was sulphated. Blocks of iduronic acid-containing repeats may contain up to five consecutive units. Alternating arrangements of iduronic acid- and glucuronic acid-containing repeats were also observed. 5. 3H- and 35S-labelled heparan sulphates from sequential extracts of fibroblasts (medium, EDTA, trypsin digest, dithiothreitol extract, cell-soluble and cell-insoluble material) afforded similar profiles after both periodate oxidation/alkaline elimination and deaminative cleavage.

Colorimetric assay of glycoprotein glycation free of interference from glycosylation residues

1993 ◽  
Vol 39 (11) ◽  
pp. 2309-2311 ◽  
Author(s):  
D M Kennedy ◽  
A W Skillen ◽  
C H Self
Keyword(s):  
Sodium Borohydride ◽  
Serum Proteins ◽  
Colorimetric Assay ◽  
Periodate Oxidation ◽  
Borohydride Reduction ◽  
Glycan Chain

Abstract We have developed a colorimetric assay for determining the degree of glycation of serum proteins that is unaffected by glycosylation residues. This was accomplished by reducing the proteins with sodium borohydride prior to periodate oxidation. Previous periodate-based methods, which offer several advantages over other glycation assays, cannot determine glycoprotein glycation because interference from sialic residues in the glycan chain can lead to overestimation of the amount of glycation products. Without reduction, glycation of fetuin was double that of asialofetuin glycated under identical conditions. We found that borohydride reduction before periodate oxidation increases the amount of formaldehyde released in proportion to the extent of glycation, irrespective of the degree of glycosylation. Using two glycoproteins and an unglycosylated protein, we showed how measurement of the formaldehyde increase enables the extent of glycoprotein glycation to be determined without removal of interfering sugars.

Chemical modification of pullulan: 1. Periodate oxidation

Polymer ◽  
1993 ◽  
Vol 34 (12) ◽  
pp. 2628-2632 ◽  
Author(s):  
Dorine Bruneel ◽  
Etienne Schacht
Keyword(s):  
Chemical Modification ◽  
Periodate Oxidation

A New Approach to 3′-Amino-3′-deoxynucleosides. Synthesis of 9-(3-Amino-3-deoxy-α-L-ribofuranosyl)adenine

1971 ◽  
Vol 49 (4) ◽  
pp. 568-573 ◽  
Author(s):  
Hans H. Baer ◽  
Monika Bayer
Keyword(s):  
Catalytic Hydrogenation ◽  
Title Compound ◽  
Condensation Product ◽  
Periodate Oxidation ◽  
Borohydride Reduction ◽  
New Approach

Methyl 2,3,4-tri-O-acetyl-6-deoxy-6-nitro-α-D-glucopyranoside (1) was acetolyzed to give 1,2,3,4-tetra-O-acetyl-6-deoxy-6-nitro-α-D-glucopyranose (2). Compound 2 (or alternatively, 6-deoxy-1,2-O-isopropylidene-6-nitro-α-D-glucofuranose 4) was converted into 2,3,4-tri-O-acetyl-6-deoxy-6-nitro-α- D-glucopyranosyl bromide (3) which was condensed with chloromercuri 6-benzamidopurine. De-O-acetylation of the condensation product 5 afforded 6-benzamido-9-(6-deoxy-6-nitro-β-D-glucopyranosyl)purine (6) which could be hydrogenated to the corresponding 6′-amino nucleoside 7. Periodate oxidation of 6 followed by internal Henry cyclization and borohydride reduction gave 6-benzamido-9-(3-deoxy-3-nitro-α-L-ribofuranosyl)purine (10) which upon catalytic hydrogenation and subsequent de-N-benzoylation produced the title compound, 12. The sensitivity of certain nitro intermediates towards alkali is commented upon.

scholarly journals Co-polymeric glycosaminoglycans in transformed cells. Transformation-dependent changes in the co-polymeric structure of heparan sulphate

1982 ◽  
Vol 201 (1) ◽  
pp. 233-240 ◽  
Author(s):  
Lars-Ȧke Fransson ◽  
Birgitta Havsmark ◽  
Vincenzo P. Chiarugi
Keyword(s):  
Heparan Sulphate ◽  
Periodate Oxidation ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Transformed Cells ◽  
Large Contribution ◽  
3T3 Cells ◽  
Normal Case ◽  
3T3 Fibroblasts ◽  
Lower Charge

1. Heparan sulphates from normal 3T3 fibroblasts are association-prone as indicated by their affinity for agarose gels substituted with cognate heparan sulphate species. Heparan sulphates from SV40-transformed or polyoma-virus-transformed cells have no affinity for the same gels. 2. Heparan sulphates from the medium, the pericellular and intracellular pools of normal, SV40-transformed and polyoma-transformed 3T3 cells were separated into four subfractions (HS1–HS4) by ion-exchange chromatography. In general, HS1–HS3 were found in cell-derived heparan sulphates, whereas HS3–HS4 were present in the medium. The heparan sulphates from transformed cells were more heterogeneous and of lower charge density than those from the normal counterpart. 3. Degradations via periodate oxidation/alkaline elimination yielded the oligomers glucosamine-(hexuronate–glucosamine)n-R with n=1–5 and a large proportion of N-sulphate groups. There was a large contribution of fragments n=4–5 from heparan sulphates of normal cells. These fragments were less common in low-sulphated heparan sulphates of transformed cells. In the case of medium-drived heparan sulphates all species had a low content of fragments n=4–5. 4. The size distribution of (glucuronate–N-acetylglucosamine)n regions was assessed after deaminative cleavage. It was broad and ranged from n=1–10 for all heparan sulphate species. In the case of medium-derived heparan sulphates there were distinct differences between normal and transformed cells. In the latter chains the N-acetyl-rich segments were both shorter and longer than in the normal case. The shape of the disaccharide peak was consistent with a lower content of O-sulphate in the heparan sulphates from transformed cells. 5. It was concluded that heparan sulphates from medium or transformed cells exhibit the greatest structural deviation from the normal case. The finding of lower proportions of extended, iduronate/glucuronate-bearing, N-sulphate-rich segments in heparan sulphates of transformed cells was particularly interesting in view of the fact that these elements have been associated with ability to self-interact.

Large heterocyclic rings from carbohydrate precursors

1969 ◽  
Vol 47 (17) ◽  
pp. 3213-3215 ◽  
Author(s):  
J. F. Stoddart ◽  
W. A. Szarek ◽  
J. K. N. Jones
Keyword(s):  
Periodate Oxidation ◽  
Borohydride Reduction

Periodate oxidation of cycloheptaamylose and cyclohexaamylose, followed by borohydride reduction and acetylation, yields 2s,4S,5R,7s,9S,10R,12s,14S,15R,17s,19S,20R,22s,24S,25R,27s,29S,30R,32s,34S,35R-heneicosaacetoxymethyl-1,3,6,8,11,13,16,18,21,23,26,28,31,33-tetradecaoxacyclopentatriacontane (2) and 2s,4S,5R,7s,9S,10R,12s,14S,15R,17s,19S,20R,22s,24S,25R,27s,29S,30R-octadecaacetoxymethyl-1,3,6,8,11,13,16,18,21,23,26,28-dodecaoxacyclotriacontane (5), respectively. Both molecules are achiral.

scholarly journals Periodate oxidation studies of human pituitary follicle-stimulating hormone

1969 ◽  
Vol 115 (2) ◽  
pp. 225-229 ◽  
Author(s):  
J. F. Kennedy ◽  
W. R. Butt
Keyword(s):  
Biological Activity ◽  
Follicle Stimulating Hormone ◽  
Periodate Oxidation ◽  
Original Material ◽  
Borohydride Reduction ◽  
Carbohydrate Component ◽  
Immunological Activity ◽  
Human Pituitary ◽  
Protein Moiety ◽  
Stimulating Hormone

A preparation of human pituitary follicle-stimulating hormone was subjected to periodate oxidation, borohydride reduction and acid hydrolysis. Comparison of the analysis of the remaining intact carbohydrate and amino acid units with the analyses of the original material and identification of the carbohydrate fragments permit some structural assignments to the molecule of follicle-stimulating hormone. The results of radioimmunological assay of fragments of the molecule of follicle-stimulating hormone suggest that, although the carbohydrate component is essential for biological activity, it is not a requirement for immunological activity, which appears to be a function of the protein moiety.

Sign in / Sign up

Export Citation Format

Share Document