Additional Precipitation Reactions of Lectins with Human Serum Glycoproteins

Abstract

Summary: Highly purified human serum glycoproteins were treated with neuraminidase and examined for their cross reaction with several lectins with anti-galactosyl specificity: )3-.D-galactosyl structures are thought to be the main terminal sugar residues that become attached de novo after removal of neuraminic acid. The following lectins were tested: Tridacnin from the bivalve clams Tridacna maxima and Tridacna gigas, the agglutinin from the sponge Axinella polypoides 9 the lectin from the roach Rutilus rutilus and the plant lectins from Ricinus communis, Ononis spinosa, Glycine soja zndAbrus precatorius. In agar gel diffusion, these purified and precipitating lectins gave more or less strong or negative results against the different neuraminidase-treated serum glycoproteins, thus indicating subtle differences with respect to their anti-galactosyl combining specificity. On the other hand, serum glycoproteins which reacted with the same lectin, did not always show complete identity lines. Finally, as revealed by these lectins, the carbohydrate moiety of serum glycoproteins may reflect a complex and broad spectrum of heterogeneity. This could lead to a more detailed understanding of the topographical and steric arrangement of the chemical structure and of the biological role of carbohydrate groups in these glycosubstances. Zusätzliche Fällungsreaktionen von Lectinen mit Glykoproteinen aus MenschenserenZusammenfassung: Menschliche Seruin-Glykoproteine wurden mit Neuraminidase behandelt und im Hinblick auf ihre Kreuzreaktionen mit verschiedenen Lectinen mit Anti-Galactosyl-Spezifität untersucht. Es wird angenommen, daß )3--D-Galactosyl-Strukturen in der Regel diejenigen Zuckerreste sind, welche nach Entfernung der Neuraminsäure endständig werden. Folgende Lectine wurden getestet: Tridacnin aus den Muscheln Tridacna maxima und Tridacna gigas, das Agglutinin vom Schwamm Axinella polypoides, das Lectin aus der Plötze Rutilus rutilus und die Pflanzenlectine oasRicinus communis, Ononis spinosa 9 Glycine sofa undAbrus precatorius. Die gereinigten, präzipitierenden Lectine gaben mehr oder weniger starke Präzipitate, wenn sie im Agargel gegen verschiedene, Neuraminidase-behandelte SerumGlykoproteine diffundierten. Auf diese Weise konnten feine Unterschiede bezüglich der Anti-Galactosyl-Spezifität aufgezeigt werden, während andererseits Serum^Glykoproteine, die mit demselben Lectin reagierten, nicht immer vollständige Identitätslinien ergäben. Die Ergebnisse deuten an, wie komplex und heterogen der Kohlenhydratanteil dieser Serum-Glykoproteine ist, wenn man um mit mehreren Lectinen untersucht. Aber nur so gewinnt man ein detailliertes Bild von der topographischen und sterischen Anordnung dieser Kohlenhydratketten in diesen Glykosubstanzeü und kann etwas über ihre Chemie und biologische Bedeutung in Erfahrung bringen.

Purified Human Plasma Proteins of Unknown Function

“…The a1M has a high affinity to polyanions , for example CM-cellulose, agar or heparin and interacts with IgG to a variable extent in the presence of calcium (Cooper and Ziccardi , 1979). Uhlenbruck et al (1978) have observed a totally unexpected precipitationreaction between a1M and asialoceruloplasmin. With regard to galactans a1M shows a calcium-dependent, lectin-like property (Uhlenbruck et al ., 1978).…”

“…Uhlenbruck et al (1978) have observed a totally unexpected precipitationreaction between a1M and asialoceruloplasmin. With regard to galactans a1M shows a calcium-dependent, lectin-like property (Uhlenbruck et al ., 1978).…”

Structure and Function of IgE Myeloma Protein VL from an Atopic Patient

“…The IgE VL has demonstrated a very high precipitating activity with all mannose-specific lectins [9] without usu ally necessary neuraminidase treatment [21]. Only 3 lectins did not show positive reaction: soybean, V. cracca and V villosa, all carrying higher specificity for D-GalNAc.…”

The use of lectins to measure acute phase proteins in the serum or plasma of man and animals during inflammation and tissue breakdown

“…The reactions with carbohydrate-containing polymers and serum glycoproteins have also been investigated and concanavalin A (con A), the Jack Bean lectin, which has a specific affinity for a-D-glucosyl residues and sterically related structures, has been found to bind and precipitate serum proteins including the acute phase reactants [3,4]. However, no attention has been paid to the value of lectin-serum glycoprotein interaction for the assessment of the biological response to physiological, pathological and 'pharmacological' agents.…”