How selective are the ?selective periodate oxidation? methods used in sialic acid histochemistry?

1991 ◽  
Vol 23 (6) ◽  
pp. 290-292 ◽  
Author(s):  
J. Needham ◽  
P. E. Reid ◽  
D. A. Owen
Keyword(s):  
Sialic Acid ◽  
Periodate Oxidation ◽  
Selective Periodate Oxidation

Characterization of surface proteins and glycoproteins on red blood cells from mice infected with haemosporidia:Plasmodium bergheiinfections of BALB/c mice

Parasitology ◽  
1980 ◽  
Vol 81 (2) ◽  
pp. 273-298 ◽  
Author(s):  
R. J. Howard ◽  
Patricia M. Smith ◽  
G. F. Mitchell
Keyword(s):  
Sialic Acid ◽  
Periodate Oxidation ◽  
Surface Protein ◽  
Surface Proteins ◽  
Red Cells ◽  
Galactose Oxidase ◽  
Infected Blood ◽  
Molecular Weights ◽  
Infected Cells

SUMMARYThe surface proteins and glycoproteins of red cells fromPlasmodium berghei-infected blood have been radio-isotope labelled and compared with those of normal mouse erythrocytes using the following protein labelling probes: lactoperoxidase-catalysed radio-iodination of tyrosyl residues, periodate oxidation and NaB3H4reduction of sialic acid and oxidation of galactosyl/N-acetylgalactosaminyl residues by galactose oxidase with subsequent NaB3H4reduction. DuringP.bergheiinfection, new tyrosyl-labelled proteins with apparent molecular weights (Mr) of 60000, 54000, 40000 and 27500 appeared on the surface of most, if not all, red cells in the blood. Purified multinucleate cells (mostly reticulocytes) differed only in that they also had a surface protein withMrof 83000. However, this molecule is thought to be specific to mouse reticulocytes rather than derived from parasites. In contrast to the relatively minor changes detected with radio-iodination, striking changes inglycoproteinradio-isotope labelling resulted from infection. All of the red cells in infected blood of greater than 20% parasitaemia lost their periodate-sensitive glycoprotein sialic acid. With some samples there was little change in glycoprotein labelling by the galactose oxidase method, provided neuraminidase was also added. Modification of the exocyclic hydroxyls of sialic acid is postulated to account for this. Other blood samples exhibited a dramatic loss of galactose oxidase-dependent labelling. It is suggested that these observations may relate to the excessive red cell destruction of uninfected as well as infected cells which has been inferred in many haemosporidial infections, including malaria.

scholarly journals A histochemical method for the identification of 9-O-acyl sialic acid. An investigation of bovine submaxillary gland and intestinal mucins.

1978 ◽  
Vol 26 (3) ◽  
pp. 187-192 ◽  
Author(s):  
P E Reid ◽  
C F Culling ◽  
W L Dunn
Keyword(s):  
Sialic Acid ◽  
Potassium Hydroxide ◽  
Periodic Acid ◽  
Periodate Oxidation ◽  
Submaxillary Gland ◽  
Sialic Acids ◽  
Histochemical Method ◽  
Periodic Acid Schiff ◽  
Oxidation Step ◽  
Intestinal Mucins

Prolongation of the initial periodate oxidation step of the periodate-borohydride technique/potassium hydroxide/periodic acid-Schiff and periodic acid-Thionin Schiff/potassium hydroxide/periodic acid-Schiff sequences produced little or no change in the diagnostic staining for the potassium hydroxide/periodic acid-Schiff effect, exhibited by the colonic epithelial mucins of man and rat and the Brunner's gland mucin of rabbits. In contrast, there was a gradual, but clear decrease in the intensity of such staining of bovine submaxillary gland mucins. It was concluded that, in the intestinal mucins studied the potassium hydroxide/periodic acid-Schiff effect was due to sialic acids bearing O-acyl substitutents at positions C7 and/or C8 whereas in bovine submaxillary gland mucin the potassium hydroxide/periodic acid-Schiff effect is probably due, at least in part, to the presence of 9-O-acyl sialic acids. This investigation has led to the development of a technique which can be used to identify 9-O-acyl sialic acids.

A new histochemical method for the selective periodate oxidation of total tissue sialic acids

1987 ◽  
Vol 19 (6-7) ◽  
pp. 311-318 ◽  
Author(s):  
D. Volz ◽  
P. E. Reid ◽  
C. M. Park ◽  
D. A. Owen ◽  
W. L. Dunn
Keyword(s):  
Periodate Oxidation ◽  
Sialic Acids ◽  
Histochemical Method ◽  
Total Tissue ◽  
Selective Periodate Oxidation

scholarly journals The copolymeric structure of pig skin dermatan sulphate. Characterization of d-glucuronic acid-containing oligosaccharides isolated after controlled degradation of oxydermatan sulphate

1974 ◽  
Vol 143 (2) ◽  
pp. 369-378 ◽  
Author(s):  
Lars-Åke Fransson ◽  
Lars Cöster ◽  
Anders Malmström ◽  
Ingrid Sjöberg
Keyword(s):  
General Formula ◽  
Glucuronic Acid ◽  
Periodate Oxidation ◽  
Dermatan Sulphate ◽  
Chondroitinase Abc ◽  
Pig Skin ◽  
Iduronic Acid ◽  
Unsaturated Disaccharide ◽  
Selective Periodate Oxidation

Selective periodate oxidation of unsubstituted l-iduronic acid residues in copolymeric dermatan sulphate chains was followed by reduction-hydrolysis or alkaline elimination. By this procedure the glucuronic acid-containing periods were isolated in oligosaccharide form; general formula: [Formula: see text] Further degradation of these oligosaccharides with chondroitinase-AC yielded three types of products: (a) sulphated trisaccharide containing an unsaturated uronosyl moiety in the non-reducing terminal and a C4 fragment in the reducing terminal, ΔUA-GalNAc-(-SO4)-R; (b) monosulphated, unsaturated disaccharide, ΔUA-GalNAc-SO4 when n is greater than or equal to 2; and (c) N-acetylgalactosamine with or without sulphate. Oligosaccharides containing a single glucuronic acid residue (n=1) comprised more than half of the glucuronic acid-containing oligosaccharides. The terminal N-acetylgalactosamine moiety of the shortest oligosaccharide was largely 4-sulphated, whereas higher oligosaccharides primarily contained 6-sulphated or unsulphated hexosamine moieties in the same position. Moreover, IdUA-SO4-containing oligosaccharides were encountered. These oligosaccharides were resistant to the action of chondroitinase-ABC.

scholarly journals The structure of a glycopeptide purified from porcine thyroglobulin

1971 ◽  
Vol 123 (3) ◽  
pp. 415-420 ◽  
Author(s):  
Minoru Fukuda ◽  
Fujio Egami
Keyword(s):  
Sialic Acid ◽  
Sodium Borohydride ◽  
Periodate Oxidation ◽  
Galactose Oxidase ◽  
Borohydride Reduction ◽  
Enzymic Hydrolysis ◽  
End Groups ◽  
Sodium Borohydride Reduction

1. The structure of a purified glycopeptide isolated from porcine thyroglobulin was studied by sequential hydrolysis with specific glycosidases, by periodate oxidation and by treatment with galactose oxidase. 2. Sequential hydrolysis with several combinations of neuraminidase, α-l-fucosidase, β-d-galactosidase, β-N-acetyl-d-glucosaminidase and α-d-mannosidase presented the evidence for the following structure. 3. The monosaccharide sequence of the peripheral moiety of the heteropolysaccharide chain was sialic acid→galactose→N-acetylglucosamine. Some of the galactose residues were non-reducing end-groups with the sequence galactose→N-acetylglucosamine. 4. After removal of the peripheral moiety composed of sialic acid, fucose, galactose and N-acetylglucosamine, α-mannosidase released 1.4mol of mannose/mol of glycopeptide, indicating that two of the three mannose residues were located between peripheral N-acetylglucosamine and internal N-acetylglucosamine or mannose. 5. Periodate oxidation and sodium borohydride reduction confirmed the results obtained by enzymic degradation and gave information concerning the position of substitution. 6. Based on the results obtained by enzymic hydrolysis and periodate oxidation together with the treatment with galactose oxidase, a structure is proposed for the glycopeptide.

scholarly journals Identification of N-acetyl-4–O-acetylneuraminyl-lactose in echidna milk

1974 ◽  
Vol 139 (2) ◽  
pp. 415-420 ◽  
Author(s):  
Michael Messer
Keyword(s):  
Sialic Acid ◽  
Acid Hydrolysis ◽  
Acid Treatment ◽  
Periodate Oxidation ◽  
Thiobarbituric Acid ◽  
Chromatographic Mobility ◽  
Mild Acid Hydrolysis ◽  
Acetylneuraminic Acid ◽  
Acid Reagent ◽  
Mild Acid

The identity of a novel form of sialyl-lactose found in milk of the echidna (Tachyglossus aculeatus) was investigated. The sialyl-lactose yielded equimolar amounts of N-acetylneuraminic acid and lactose during mild acid hydrolysis but was resistant to the action of a bacterial neuraminidase. A viral neuraminidase hydrolysed it to lactose plus a form of sialic acid that reacted positively with thiobarbituric acid reagent but whose chromatographic mobility was greater than that of N-acetylneuraminic acid. Treatment with alkali converted the sialyl-lactose into a substance with the same chromatographic mobility as N-acetylneuraminyl-(2→3)-lactose and made it susceptible to the action of bacterial neuraminidase. The sialyl-lactose contained one mol of ester (identified as acetyl), and released one mol of formaldehyde during periodate oxidation, per mol of sialic acid. It did not contain N-glycollylneuraminic acid. These results indicate that the sialyl-lactose is N-acetyl-4-O-acetylneuraminyl-(2→3)-lactose. Echidna milk contained, in addition, a small amount of N-acetylneuraminyl-(2→3)-lactose.

Structure determination ofStreptococcus suisserotype 2 capsular polysaccharide

2010 ◽  
Vol 88 (3) ◽  
pp. 513-525 ◽  
Author(s):  
Marie-Rose Van Calsteren ◽  
Fleur Gagnon ◽  
Sonia Lacouture ◽  
Nahuel Fittipaldi ◽  
Marcello Gottschalk
Keyword(s):  
Sialic Acid ◽  
Capsular Polysaccharide ◽  
Group B Streptococcus ◽  
Periodate Oxidation ◽  
Methylation Analysis ◽  
Mild Acid Hydrolysis ◽  
Chemically Modified ◽  
Group B ◽  
Suis Serotype ◽  
Mild Acid

The capsular polysaccharide (CPS) of Streptococcus suis serotype 2 was isolated, purified, chemically modified, and characterized. Sugar and absolute configuration analyses of the CPS gave the following composition: d-Gal, 3; d-Glc, 1; d-GlcNAc, 1; d-Neu5Ac, 1; l-Rha, 1. Sialic acid was found to be terminal, and the CPS was quantitatively desialylated by mild acid hydrolysis. The CPS was also submitted to periodate oxidation followed by borohydride reduction and Smith degradation. Sugar and methylation analysis,1H and13C nuclear magnetic resonance, and mass spectrometry of the native CPS or of its specifically modified products allowed to determine the repeating unit sequence: [4)[Neu5Ac(α2–6)Gal(β1–4)GlcNAc(β1–3)]Gal(β1–4)[Gal(α1–3)]Rha(β1–4)Glc(β1-]n. The backbone sequence was found to be identical to that of Streptococcus agalactiae or group B Streptococcus (GBS) type VIII and Streptococcus pneumoniae type 23F. The S. suis CPS shares the sequence Neu5Ac-Gal-GlcNAc-Gal in common with GBS types Ia, Ib, II, III, and IV CPSs but differs from them by the presence of rhamnose and the fact that sialic acid is 2,6- rather than 2,3-linked to the following Gal. A correlation between the S. suis CPS sequence and genes of the serotype 2 cps locus encoding putative enzymes responsible for the biosynthesis of the repeating unit was tentatively established.

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