Surface engineering of living myoblasts via selective periodate oxidation

2003 ◽  
Vol 81 (7) ◽  
pp. 800-808 ◽  
Author(s):  
P. A. De Bank ◽  
B. Kellam ◽  
D. A. Kendall ◽  
K. M. Shakesheff
Keyword(s):  
Surface Engineering ◽  
Periodate Oxidation ◽  
Selective Periodate Oxidation

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

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 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 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.

Cytochemical Studies of Cell Wall Biosynthesis in Staphylococcus Aureus

1972 ◽  
Vol 30 ◽  
pp. 328-329
Author(s):  
Masaatsu Koike ◽  
Koichi Nakashima ◽  
Kyoko Iida
Keyword(s):  
Staphylococcus Aureus ◽  
Periodate Oxidation ◽  
Early Time ◽  
The Other ◽  
Penicillin G ◽  
Cell Wall Biosynthesis ◽  
Septal Wall ◽  
Peptidoglycan Biosynthesis ◽  
Gram Positive Bacteria ◽  
Cross Linkage

Penicillin exerts the activity to inhibit the peptide cross linkage between each polysaccharide backbone at the final stage of wall-peptidoglycan biosynthesis of bacteria. Morphologically, alterations of the septal wall and mesosome in gram-positive bacteria, which were occurred in early time after treatment with penicillin, have been observed. In this experiment, these alterations were cytochemically investigated by means of silver-methenamine staining after periodate oxidation, which is applied for detection of localization of wall mucopolysaccharide.Staphylococcus aureus strain 209P treated with 100 u/ml of penicillin G was divided into two aliquotes. One was fixed by Kellenberger-Ryter's OSO4 fixative at 30, 60 and 120 min after addition of the antibiotic, dehydrated through alcohol series, and embedded in Epon 812 (Specimen A). The other was fixed by 21 glutaraldehyde, dehydrated through glycolmethacrylate series and embedded in glycolmethacrylate mixture, according to Bernhard's method (Specimen B).

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