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 A new histochemical method for detection of sialic acids using a physical development procedure.

1995 ◽  
Vol 43 (10) ◽  
pp. 1045-1051 ◽  
Author(s):  
T Ueda ◽  
O Fujimori ◽  
K Yamada
Keyword(s):  
Periodic Acid ◽  
Periodate Oxidation ◽  
Physical Development ◽  
Sialic Acids ◽  
New Method ◽  
Histochemical Method ◽  
Reaction Products ◽  
Specificity And Sensitivity ◽  
Development Procedure ◽  
Selective Periodate Oxidation

We have established an efficient histochemical method for demonstration of sialic acids in light microscopy. The method consists of a selective periodate oxidation-phenylhydrazine blockade and a thiocarbohydrazide-silver protein sequence followed by a physical development procedure. From the results obtained by the present experimental and control studies in tissue sections from a series of rat and mouse organs, such as stomach, duodenum, colon, liver, sublingual gland, lung, and kidney, the specificity and sensitivity of the method were sufficient. In the tissues tested, sialic acids were visualized as distinct brownish and blackish reaction products. Comparisons of the new method with the periodic acid-phenylhydrazine-Schiff (PA-P-S) or selective periodate oxidation-Schiff (PA*-S) method employed hitherto have confirmed that the new method reported here is higher in efficiency and visibility of reaction products than the latter two methods.

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.

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

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 A new histochemical method for the identification and visualization of both side chain acylated and nonacylated sialic acids.

1976 ◽  
Vol 24 (12) ◽  
pp. 1225-1230 ◽  
Author(s):  
C F Culling ◽  
P E Reid ◽  
W L Dunn
Keyword(s):  
Potassium Hydroxide ◽  
Periodic Acid ◽  
Sialic Acids ◽  
Histochemical Method ◽  
Side Chain ◽  
Parotid Glands ◽  
Periodic Acid Schiff ◽  
Mucin Histochemistry ◽  
Single Section ◽  
General Field

A new histochemical method is described for the differentiation of mucins that utilizes two different Schiff reagents and allows single section identification of side chain O-acylated, and nonacylated, sialic acids in contrasting colors. In the event of mucins containing only one type of sialic acid, it may allow their specific identification (e.g., C7 or C8 side chain O-acylated). It has been shown to be useful in the identification of some metastases from adenocarcinomas of colon (where the primary is potassium hydroxide/periodic acid-Schiff positive) and should prove of great value in the investigation of diseases of the gastrointestinal tract and particularly those of the colon. It should also be valuable in the general field of epithelial mucin histochemistry, particularly for those mucins of the salivary and parotid glands, etc.

scholarly journals A method for the sequence analysis of dermatan sulphate

1990 ◽  
Vol 269 (2) ◽  
pp. 381-388 ◽  
Author(s):  
L Å Fransson ◽  
B Havsmark ◽  
I Silverberg
Keyword(s):  
Periodate Oxidation ◽  
Amino Group ◽  
Serine Residue ◽  
Dermatan Sulphate ◽  
Pig Skin ◽  
Complete Digestion ◽  
Chondroitin Ac Lyase ◽  
Beta Galactosidase ◽  
Selective Periodate Oxidation ◽  
Testicular Hyaluronidase

We are attempting to develop methods for the sequencing of glycosaminoglycans from their reducing end. Here we describe a procedure for the analysis of dermatan sulphate from pig skin. The glycosaminoglycan is released from its parent proteoglycan by exhaustive proteolysis by using both endo- and exo-peptidases. The amino group of the residual serine residue is conjugated with a p-hydroxyphenyl group, which in turn is iodinated with 125I (the Bolton-Hunter reagent, BHR). The ion-exchange-purified end-labelled dermatan sulphate is then degraded partially or completely by various enzymic or chemical means to yield fragments extending from the labelled serine residue to the point of cleavage. The various products are separated by gradient PAGE, detected by autoradiography and quantified by videodensitometry. Complete digestion with chondroitin ABC lyase affords the labelled fragment delta HexA-GalNAc(-SO4)-GlcA-Gal-Gal-Xyl-Ser(-BHR). The structure was confirmed by sequential degradation from the non-reducing end by chondroitin AC lyase, HgCl2, and beta-galactosidase. Periodate oxidation cleaves most of the Xyl even without treatment with alkaline phosphatase, showing that Xyl is not substituted with phosphate. Results from partial and selective periodate oxidation indicate that most of the non-sulphated IdoA residues are located towards the non-reducing end. Partial or complete digestions with testicular hyaluronidase (in the presence of an excess of beta-glucuronidase) or chondroitin AC lyase identify the positions of GlcA residues. The results confirm that HexA next to Gal is always GlcA. Moreover, GlcA is common in the first three disaccharide repeats. Results with testicular hyaluronidase indicate that the distribution of clustered GlcA-GalNAc repeats is periodic and peaks at positions 1-3, 8-9 and around 25. Although there must be chains that contain IdoA in nearly all of the available positions, regions that have not been fully processed during biosynthesis are markedly non-random.

scholarly journals A detailed study of the periodate oxidation of sialic acids in glycoproteins

1989 ◽  
Vol 6 (1) ◽  
pp. 35-44 ◽  
Author(s):  
Gerd Reuter ◽  
Roland Schauer ◽  
Claudia Szeiki ◽  
Johannis P Kamerling ◽  
Johannes FG Vliegenthart
Keyword(s):  
Periodate Oxidation ◽  
Sialic Acids
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