Table Of ContentAdvances in Lectin Research Volume4
To Josephine
* 28. 12. 1990
Advances in
Lectin Research
Volume4
Edited by Hartmut Franz
Coeditors: Ken-ichi Kasai, Jan Kocourek,
Sjur Olsnes, Leland M. Shannon
With 40 Figures and 13 Tables
Springer-Verlag Berlin Heidelberg GmbH
Hartmut Franz
Staatliches lnstitut fiir lmmunpraparate und Niihrmedien
Klement-Gottwald-Allee 317-321, Berlin,
0 -1120, Germany
Ken-ichi Kasai
Faculty of Pharmaceutical Sciences,
Teikyo University
Sagamiko, Kanagawa 199-01,
Japan
Jan Kocourek
Dept. of Biochemistry Charles University Prague
Hrusicka 2515, 14100 Praha 4-Spofilov 11,
Czechoslovakia
SjurOlsnes
Norsk Hydro's Institute for Cancer Research
Montebello Oslo 3,
Norway
Leland M. Shannon
University of Califomia
Riverside, California 92521,
USA
Adv;mces in Lectin Research. Volume 4 I hrsg. v. H. Franz. -
ISBN 978-3-333-00584-3 ISBN 978-3-662-26751-6 (eBook)
DOI 10.1007/978-3-662-26751-6
1.Auflage
© Springer-Verlag Berlin Heidelberg 1991
Originally published by Springer-Verlag in 1991
Softcover reprint of the hardcover 1st edition 1991
Dieses Werk ist urheberrechtlich geschiitzt. Die daraus begriindeten Rechte, insbesondere die der Uber
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Satz: Forster & Borries Satz-Repro-GmbH Zwickau
Authors
Prof. Dr. Henri Deb ray
Universite des Sciences et Techniques de Lille Flanders-Artois
Laboratoire de Chimie Biologique
59655 Villeneuve d'Ascq Cedex, France
Dr. Christian Flemming
Institut fiir Biotechnologie
Permoserstr. 15, Leipzig, 0-7050, Germany
Prof. Dr. Dr. Hartmut Franz
Staatliches Institut fiir Immunpraparate und Nahrmedien
Klement-Gottwald-Allee 317-321, Berlin, 0-1120, Germany
Dr. J. Montreuil
Universite des Sciences et Techniques de Lille Flanders-Artois
Laboratoire de Chimie Biologique
59655 Villeneuve d'Ascq Cedex, France
Prof. Dr. Gerhard Uhlenbruck
Universitatskliniken Ki:iln
Abteilung Immunologie
Kerpener StraBe 15, Ki:iln 41, W-5000, Germany
From the Foreword to Volume 1
The years 1987/88 appear to be a suitable moment for the publication of"Advances in Lectin Re
search". The detection of ricin 100 years ago led to interesting results conceming sugar-binding
proteins, now called lectins. Today two main lines exist in "lectinology". Firstly, lectins are used
as multi-purpose tools (analysis and isolation of glycoconjugates, characterization and prepara
tion of cells and microorganism, lectin histochemistry). Secondly, lectins are of interest concer
ning their physiological roles and other biological activities. Espedally during the last 10 years,
the latter aspects have been widely noticed. More and more the opinion is being accepted that
lectins are glues of moderate affinity, making possible the contact of biologically cooperating gly
coconjugates and cells bearing glycoconjugates.
The results of lectin research anticipated for the coming years should be of great importance not
only for basic research, but also for diagnostic and even therapeutic application (adherence inhi
bition of bacteria and tumor cells, immunomodulation, lectin-mediated cytotoxicity, chemically
modified toxic lectins) ...
"Advances in Lectin Research", as a collection of review articles, is not in competition with text
books and congress proceedings ...
Foreword to Volume 4
Following the now proved principles of the former volumes of "Advances in Lectin Research" we
present in volume 4 again articles covering the diversity of present lectinology. The editor hopes
for further comments and for advices. He has to thank both the Verlag Gesundheit GmbH and
the Springer-Verlag, the coeditors and again Mrs. Margitta Hintz, Dr. Rolf Wachowius, Heinz
Zom and Mrs. Marianne Lob stein.
Hartmut Franz, Berlin
Contents
Lectinology on the Threshold of Its Second Century 11
Hartmut Franz
1 The Tridacna Lectins 13
Gerhard Uhlenbruck
1.1 Introduction: Historical Background 13
1.2 The Discovery of Tridacna Lectins 13
1.3 The Source of Tridacna Lectins: The Tridacna Clam 15
1.4 The Purification of Tridacna Lectins 16
1.5 Precipitin Reactions of Tridacna Lectins 16
1.6 Practical Use of the Precipitin Reactions 20
1.7 Agglutination Pattems of Tridacna Lectins 21
1.8 Mitogenic Properties of Tridacna Lectins 22
1.9 The Receptor Site of Tridacna Lectins 25
1.10 Cross-Reacting Lectins and Antibodies 26
1.11 The Biological Role of Tridacna Lectins 27
1.12 References 28
2 Mistletoe Lectins (2) 33
Hartmut Franz
2.1 Introduction 33
2.2 · Cytotoxicity 33
2.3 In Vivo Toxicity 34
2.4 Mistletoe Lectins and Cancer Therapy 36
2.4.1 Release ofiL-1 and IL-2 36
2.4.2 Release of C-Reactive Protein 36
2.4.3 Cell Activation by Viscum album Preparations 38
2.4.4 Mistletoe Lectins and Breast Cancer. Histochemical Investigations 39
2.4.5 lmmunotoxins Containing the A Chain ofMLI 41
2.5 Lectin/Sugar Interactions in Nonpolar Solvents 41
2.6 Ligand Leakage from MLIMfinity Columns 43
2.7 Conformation of MLI at Different pH 43
2.8 Further Characterization of ML I, ML II, and ML ill 43
2.9 Concluding Remarks 45
2.10 References 45
8
Lectin Affinity Chromatography of Glycoconjugates 51
H. Deb ray and J. Montreuil
3.1 Introduction 51
3.1.1 Type of Glycans That Lectins Can Recognize at the Cell Surface 51
3.1.2 Problems of Lectin Specificity 54
3.1.2.1 Lectins Can Interact with Internal Sequences of an Oligosaccharide 55
3.1.2.2 Lectins, Identical in Terms of Monosaccharide Specificity, Can Possess Different
"Complex" Specificities 56
3.1.2.3 Importance of the Spatial Conformation of Glycans in the Interaction with Lectins 56
3.1.3 Conclusions 58
3.2 Use of Immobilized Lectins for Fractionation of Glycoproteins 58
3.2.1 Immobilization of Lectins 58
3.2.2 Use of Immobilized Lectins for Purification of Soluble Glycoproteins 59
3.2.2.1 Use of Crossed lmmunoaffinity Electrophoresis of Glycoproteins as a Guide
to Lectin Mfinity Chromatography 59
3.2.2.2 Binding Capacity of the Immobilized Lectins and Problems of the Elution 60
3.2.2.3 Sequential Mfinity Chromatography of Soluble Glycoproteins on Different
Immobilized Lectins 61
3.2.2.4 Development of High Performance Mfinity Chromatography Using Immobilized
Lectins 62
3.2.3 Use of Immobilized Lectins for Fractionation of Membrane Glycoproteins 62
3.2.4 Limitations of Lectin Affinity Chromatography for Purification of Soluble and
Membrane Glycoproteins 64
3.3 Use of Immobilized Lectins for Fractionation of Glycopeptides and
Oligosaccharides 65
3.3.1 Introduction 65
3.3.2 Fractionation of N -Glycosylpeptides Using Immobilized Lectins with Mfinity
for lntemal Saccharidic Sequences 65
3.3.2.1 Mfinity Chromatography on Immobilized Concanavalin A 65
3.3.2.2 Mfinity Chromatography on Immobilized Lens culinaris Agglutinin 68
3.3.2.3 Mfinity Chromatography on Other Lectins with a Specificity for lntemal Saccharidic
Sequences 68
3.3.3 Subfractionation of N-Glycosylpeptides Using Lectins with a Specificity Directed
Toward Terminal Dominant-Oligosaccharidic Sequences 74
3.3.3.1 Subfractionation of Poly(N -Acetyllactosamine )-Type N -Glycosylpeptides and
Related Oligosaccharides 74
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