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.

Immunological investigations of Penicillium.: I. Serological reactivities of exocellular polysaccharides produced by six Penicillium species

1970 ◽  
Vol 16 (8) ◽  
pp. 687-694 ◽  
Author(s):  
J. F. Preston III ◽  
Erlinda Lapis ◽  
J. E. Gander
Keyword(s):  
Acid Hydrolysis ◽  
Acid Treatment ◽  
Cross Reactivity ◽  
Antigenic Specificity ◽  
Mild Acid Hydrolysis ◽  
Penicillium Species ◽  
Whole Cells ◽  
Exocellular Polysaccharides ◽  
Antigenic Reactivity ◽  
Mild Acid

The exocellular polysaccharides of Penicillium charlesii, P. chrysogenum, P. raistrickii, P. claviforme, and P. patulum contain galactofuranosyl residues since galactose is released by mild acid hydrolysis. Antisera from rabbits injected with whole cells of P. charlesii cross reacted with the exocellular polysaccharides from each species. The exocellular polymer from Penicillium various contained no galactose labile to mild acid treatment, and showed no cross reactivity with antisera to P. charlesii. No antigenic reactivity was observed in exocellular polysaccharides modified by mild acid hydrolysis. Oligosaccharides produced by mild acid hydrolysis which contained galactofuranosyl moieties as well as methyl α-D- and methyl β-D-galactofuranosides inhibited precipitate formation when the antigen was incubated with antisera. Treatment of the polysaccharides with 1 N NaOH did not alter its reactivity toward the antisera. It was concluded that several species of Penicillium elaborate exocellular polysaccharides containing galactofuranosyl residues and that these residues contribute to the antigenic specificity of the organism.

scholarly journals IMMUNOCHEMICAL STUDIES ON BLOOD GROUPS

1971 ◽  
Vol 133 (1) ◽  
pp. 39-52 ◽  
Author(s):  
Ten Feizi ◽  
Elvin A. Kabat ◽  
Giuseppe Vicari ◽  
Byron Anderson ◽  
W. Laurence Marsh
Keyword(s):  
Acid Hydrolysis ◽  
Blood Group ◽  
Ovarian Cyst ◽  
Periodate Oxidation ◽  
Human Saliva ◽  
Mild Acid Hydrolysis ◽  
Group B ◽  
Hydrolysis Of ◽  
Substantial Heterogeneity ◽  
Mild Acid

A partially purified blood group-like substance obtained from milk showed I activity with 2 of 21 anti-I sera. With these antisera, certain human ovarian cyst substances considered to be precursors of the A, B, H, Lea, and Leb substances also showed I activity comparable to the milk material. Strong I activity could be produced by one-stage periodate oxidation and Smith degradation of human ovarian cyst A and B substances, or of hog mucin A + H substance, or by mild acid hydrolysis of human saliva or ovarian cyst blood group B substance. The two sera indicate that I specificity appears at intermediate stages in the biosynthesis of the A, B, H, Lea, and Lea substances. Anti-I sera differ strikingly in their specificities, indicating substantial heterogeneity of the I determinants.

scholarly journals Guinea-pig kidney β-N-acetylgalactosaminyltransferase towards Tamm-Horsfall glycoprotein. Requirement of sialic acid in the acceptor for transferase activity

1983 ◽  
Vol 215 (3) ◽  
pp. 483-489 ◽  
Author(s):  
F Serafini-Cessi ◽  
F Dall'Olio
Keyword(s):  
Sialic Acid ◽  
Guinea Pig ◽  
Acid Hydrolysis ◽  
Transferase Activity ◽  
Carbohydrate Composition ◽  
Mild Acid Hydrolysis ◽  
Enzymic Digestion ◽  
Pig Kidney ◽  
Mild Acid

A beta-N-acetylgalactosaminyltransferase that preferentially transferred N-acetylgalactosamine to Sd(a-) Tamm-Horsfall glycoprotein was found in guinea-pig kidney microsomal preparations. This enzyme was kidney-specific and was able to transfer the sugar to other glycoproteins, such as fetuin and alpha 1-acidic glycoprotein. The presence of sialic acid in the acceptors was essential for the transferase activity when either glycoproteins or their Pronase glycopeptides were used as acceptors. Two glycopeptides (Tamm-Horsfall glycopeptides I and II) with a different carbohydrate composition were separated by DEAE-Sephacel chromatography from Pronase-digested Tamm-Horsfall glycoprotein. The amount of N-acetylgalactosamine transferred to glycopeptides by the enzyme correlated with their degree of sialylation. Enzymic digestion of N-[14C]acetylgalactosamine-labelled Tamm-Horsfall glycopeptide II showed that the transferred sugar was susceptible to beta-N-hexosaminidase. The amount of sugar cleaved by beta-hexosaminidase was strongly increased when the labelled Tamm-Horsfall glycopeptide II was pretreated with mild acid hydrolysis, a procedure that removed the sialic acid residues. Alkaline borohydride treatment of the labelled Tamm-Horsfall glycopeptide II did not release radioactivity, thus indicating that enzymic glycosylation took place at the N-asparagine-linked oligosaccharide units of Tamm-Horsfall glycoprotein.

scholarly journals The influence of sialic acid residues on the ability of glycoproteins toi nteract electrostatically with chondromucoprotein

1965 ◽  
Vol 97 (2) ◽  
pp. 333-339 ◽  
Author(s):  
AJ Anderson
Keyword(s):  
Sialic Acid ◽  
Complex Formation ◽  
Acid Hydrolysis ◽  
Acid Content ◽  
Biological Activities ◽  
Carbohydrate Composition ◽  
Mild Acid Hydrolysis ◽  
Sialic Acid Content ◽  
Neuraminidase Treatment ◽  
Mild Acid

1. Although glycoproteins with less than 1% of sialic acid (fibrinogen, lipoproteins, gamma-globulins) interact electrostatically with chondromucoprotein to form insoluble complexes, interaction with glycoproteins containing larger amounts of sialic acid (orosomucoid, urine glycoprotein, seromucoid, fraction VI) was electrostatically impossible. Reasons for this are discussed. 2. The latter glycoproteins interacted with chondromucoprotein after mild acid hydrolysis or neuraminidase treatment, complex-formation being inversely related to their sialic acid content. 3. Complex-formation with sialic acid-deficient orosomucoid was maximum at pH3.6 and negligible above its isoelectric point of pH5, and was inhibited by Ca(2+) ions and EDTA. 4. These results are discussed in relation to the carbohydrate composition and biological activities of euglobulin fractions, and of complexes formed by adding chondromucoprotein to abnormal plasmas which may contain sialic acid-deficient glycoproteins owing to faulty carbohydrate metabolism.

THE WATER-SOLUBLE POLYSACCHARIDES OF DERMATOPHYTES: III. A GALACTOMANNAN FROM TRICHOPHYTON INTERDIGITALE

1964 ◽  
Vol 42 (12) ◽  
pp. 2862-2871 ◽  
Author(s):  
F. Blank ◽  
M. B. Perry
Keyword(s):  
Formic Acid ◽  
Acid Hydrolysis ◽  
Copper Complex ◽  
Periodate Oxidation ◽  
Water Soluble ◽  
Mild Acid Hydrolysis ◽  
Trichophyton Interdigitale ◽  
Soluble Polysaccharide ◽  
Hydrolysis Of ◽  
Mild Acid

The water-soluble polysaccharide preparation from Trichophytoninterdigitale was fractionated to give two distinct galactomannans and a glucan. A galactomannan isolated via its insoluble copper complex had [α]D +75° (water) and was composed of D-galactose (12%) and D-mannose (88%). On periodate oxidation, the galactomannan consumed 1.73 mole periodate and released 0.67 mole formic acid and 0.12 mole formaldehyde per anhydrohexose unit. Hydrolysis of the methylated galactomannan gave 2,3,5,6-tetra-O-methyl-D-galactose (1 part), 2,3,4,6-tetra-O-methyl-D-mannose (1 part), 2,3,4-tri-O-methyl-D-mannose (4 parts), and3,4-di-O-methyl-D-mannose (2 parts). Mild acid hydrolysis of the galactomannan removed all the galactose residues, leaving a mannan having [α]D +84° (water) whose structure was analyzed by periodate oxidation and methylation techniques.

THE STRUCTURAL ANALYSIS OF SOME ACIDIC XYLANS BY PERIODATE OXIDATION

1962 ◽  
Vol 40 (2) ◽  
pp. 348-352 ◽  
Author(s):  
G. G. S. Dutton ◽  
A. M. Unrau
Keyword(s):  
Acid Hydrolysis ◽  
Glucuronic Acid ◽  
Periodate Oxidation ◽  
Small Degree ◽  
Degree Of Polymerization ◽  
Borohydride Reduction ◽  
Mild Acid Hydrolysis ◽  
Degree Of Branching ◽  
Hydrolysis Of ◽  
Mild Acid

By determining the amount of formaldehyde produced on periodate oxidation of borohydride-reduced apple- and cherry-wood xylans the degree of polymerization was shown to be 155 and 100 respectively. Acid hydrolysis of the polyols obtained by periodate oxidation and borohydride reduction gave ethylene glycol in amounts indicating that these xylans have a small degree of branching. Mild acid hydrolysis of the polyols demonstrated that in these xylans D-glucuronic acid as well as 4-O-methyl-D-glucuronic acid was present and that some of the former occupied non-terminal positions.

A method for the simultaneous estimation of free and ketosidically bound sialic acids

1977 ◽  
Vol 55 (7) ◽  
pp. 778-782 ◽  
Author(s):  
C. F. A. Culling ◽  
P. E. Reid ◽  
C. W. Ramey ◽  
W. L. Dunn ◽  
M. G. Clay
Keyword(s):  
Sialic Acid ◽  
Room Temperature ◽  
Thiobarbituric Acid ◽  
Sialic Acids ◽  
Simultaneous Estimation ◽  
Sodium Metaperiodate ◽  
Acetylneuraminic Acid ◽  
Acid Reagent ◽  
Bovine Submaxillary Mucin ◽  
Free Sialic Acid

Various methods for the estimation of free and ketosidically bound sialic acid were investigated for accuracy and specificity. It was found that oxidation with 0.025 M sodium metaperiodate in pH 7.0 phosphate buffer at room temperature for 20 min provided a simple, rapid, sensitive method whereby both the free and the ketosidically bound acid present in a mixture could be quantitatively analyzed. On completion of the oxidation step, the bound sialic acid is estimated with resorcinol reagent and the free sialic acid with thiobarbituric acid reagent. Oxidation under these conditions permitted a facile analysis of mixtures of bovine submaxillary mucin and free N-acetylneuraminic acid, whereas the Warren thiobarbituric acid procedure gave an erroneous value for free sialic acid.

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.

GUM JEOL: THE STRUCTURE OF THE DEGRADED GUM DERIVED FROM IT

1964 ◽  
Vol 42 (1) ◽  
pp. 107-112 ◽  
Author(s):  
A. K. Bhattacharyya ◽  
C. V. N. Rao
Keyword(s):  
Acid Hydrolysis ◽  
Galacturonic Acid ◽  
Uronic Acid ◽  
Periodate Oxidation ◽  
Neutral Fraction ◽  
Partial Structure ◽  
Mild Acid Hydrolysis ◽  
Acidic Fraction ◽  
Hydrolysis Of ◽  
Mild Acid

Gum Jeol has been shown to be composed of residues of D-galactose, L-arabinose, and D-galacturonic acid. On mild acid hydrolysis the gum gave an aldobiouronic acid, viz. 3-O-(D-galactopyranosyl uronic acid)-D-galactopyranose. Hydrolysis of the fully methylated degraded gum yielded 2,3,4,6-terra-(3 moles); 2,3,4-tri-(2 moles); 2,4-di-(1 mole); and 2-O-methyl-D-galactose (1 mole) in the neutral fraction of the hydrolyzate. The reduced acidic fraction yielded 2,3,4-tri-(2 moles) and 2,4-di-O-methyl-D-galactose (2 moles). Based on these results a partial structure of the degraded gum has been proposed, the additional evidence of which was deduced from periodate oxidation studies of the degraded gum.

Convenient preparation of a crystalline derivative of meso-tartraldehyde

1965 ◽  
Vol 18 (12) ◽  
pp. 1973 ◽  
Author(s):  
SJ Angyal ◽  
SD Gero
Keyword(s):  
Acid Hydrolysis ◽  
Periodate Oxidation ◽  
Mild Acid Hydrolysis ◽  
Convenient Preparation ◽  
Mild Acid

Periodate oxidation of 1,2-O-cyclohexylidenemyoinositol gives cis-3,4-cyclohexylidenedioxy-2,5-dihydroxytetrahydrofuran (III), a compound which liberates meso-tartraldehyde on mild acid hydrolysis. Condensation with nitromethane provides a synthesis of 5-nitrocyclopentane-1,2,3,4-tetraols.

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