Effect of sialidase on blood group specificity of hog submaxillary glycoproteins

Aminoff, David; Morrow, Marianne P.

doi:10.1016/0014-5793(90)80012-8

Cited by 15 publications

(5 citation statements)

References 14 publications

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“…3). The PSM preparation used in this study was found to be inhibitory only against Cytisus sessilifolius hemagglutinin and Ulex hemagglutinin II and was there fore considered to be of the so-called In group [1]. Treatment of the glycoprotein with neuraminidase from Vibrio cholerae or Clostridium perfringens gave rise to inhibitory activity against eel serum and Laburnum alpinum hemagglutinins.…”

Section: Resultsmentioning

confidence: 82%

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On the Specificity of Various Heterologous Anti-H Hemagglutinins

Matsumoto¹

1971

Vox Sanguinis

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Inhibition assays against various anti-H hemagglutinins were undertaken utilizing oligosaccharides from human milk, various aryl β-D-glycosides, blood group substances and their enzymic hydrolysis products. While anti-H hemagglutinins can be subdivided into two groups, eel serum-type and Cytisustype hemagglutinins, on the basis of inhibition assays with simple sugars such as L-fucose and di-N-acetylchitobiose, evidence for differences of specificity even among the same group of hemagglutinins is presented and discussed.

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Section: Resultsmentioning

confidence: 82%

“…On the other hand, Cytisustype hemagglutinins are inhibited best by di-N-acetylchitobiose [16,23], the structure of which is not found in the carbohydrate chain of any blood group determinant structure. Thus, the structure with 1 Supported by a research grant from the Ministry of Education of Japan.…”

Section: Introductionmentioning

confidence: 99%

On the Specificity of Various Heterologous Anti-H Hemagglutinins

Matsumoto¹

1971

Vox Sanguinis

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“…The appropriate corrections were applied to the quantitation of the sialic acid released in accordance with the different intensities of color given by the two sialic acids in the resorcinol and TBA assays (32).…”

Section: Amount and Type Of Sialic Acid Released From Erythrocytes Ofmentioning

confidence: 99%

Effect of sialidase on the viability of erythrocytes in circulation

et al. 1976

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Sialic acid has been detected on the erythrocyte surface of a number of different species of animals. The objective of this investigation was to determine the physiological significance of these sialyl residues to the viability of erythrocytes in circulation. Methods have been described for the determination of total sialic acid on red blood cells and the conditions under which it may be released with sialidase. Chicken, dog, goat, and rabbit were chosen for these studies because of the differences in the amount (3 X 10(6) - 72 X 10(6) resides per erythrocyte), and type (N-acetyl-or N-glycolyl-neuraminic acids) of sialic acid found on the surface of their erythrocytes. Radioactive tagging with Na251CrO4 was used to monitor the effect of sialidase on the viability of erythrocytes upon autologous transfusion. By the two criteria used to assess the viability of erythrocytes-the percentage of erythrocytes surviving 24 hr after the autologous transfusion, and the half-life of those red blood cells in circulation that survive the first 24 h after the autologous transfusion, and the half-life of those red blood cells in circulation that survive the first 24 hr-it is apparent that the presence of sialic acid on the cell surface is crucial for the survival of nonnucleated mammalian erythrocytes. The loss of viability of dog erythrocytes can be elicited by the removal of approximately 10% of the total sialic acid. In marked contrast to the behavior of mammalian erythrocytes, sialidase-treated chicken erythrocytes appear to retain their viability in circulation.

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“…Hog submaxillary glycoproteins used for the assay of the sialidase and a-l,2-L-fucosidase were prepared by modifications of the procedures described elsewhere [12,13]. Desialyzed ovine submaxillary glycoprotein used for the assay of the a-N-acetylgalactosaminidase was prepared by acid hydrolysis (0.1 M HC1, 80 °C, 45 min) of ovine submaxillary glycoprotein [14]. Sialic acid (NAN), fucose and p-nitrophenyl glycosides were obtained commercially as previously described [7].…”

Section: Methodsmentioning

confidence: 99%

Non-specific protein binding by adsorbents designed for the specific affinity chromatography of sialidase in crude bacterial extracts

Huang

Aminoff

1974

Biochimica et Biophysica Acta (BBA) - Protein Structure

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A number of derivatives of Sepharose 4B gels were prepared containing tyramine,-Gly-Gly-Tyr and the tetrapeptide, Thr (But)-Phe-Pro-Tyr-. A specific inhibitor of sialidase, p-diazo-phenyl oxamic acid, was also coupled to these phenolsubstituted Sepharose gels. The effectiveness of these gels to purify sialidase by "affinity" chromatography was examined. The sialidase from Vibrio cholerae was adsorbed by these gels and subsequently re-eluted by a change in pH and temperature. The adsorption and elution of enzyme was independent of the presence or absence of the "specific inhibitor" of the sialidase, phenyl oxamic acid. A mechanism for the adsorption and subsequent elution of the sialidase is proposed. It is important to re-evaluate the biological data obtained with sialidase prepared by the affinity column recommended by Cuatrecasas and Illiano, Biochem. Biophys. Res. Commun. 44, 178-184 (1971), since glycosidases from Clostridium perfringens other than sialidase are also adsorbed and eluted under the conditions specified.

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Effect of sialidase on blood group specificity of hog submaxillary glycoproteins

Cited by 15 publications

References 14 publications

On the Specificity of Various Heterologous Anti-H Hemagglutinins

On the Specificity of Various Heterologous Anti-H Hemagglutinins

Effect of sialidase on the viability of erythrocytes in circulation

Non-specific protein binding by adsorbents designed for the specific affinity chromatography of sialidase in crude bacterial extracts

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