Chapter 1 Chairman's advent (pages 1–2): A. J. Kenny
Chapter 2 Introductory comments at the Brush Border (pages 3–11): D. S. Parsons
Chapter three Microvillar Endopeptidase, An Enzyme with certain Topological positive factors and a large Distribution (pages 12–33): A. John Kenny and Ian S. Fulcher
Chapter four Aminopeptidases and Proteolipids of Intestinal Brush Border (pages 34–49): S. Maroux, H. Feracci, J. P. Gorvel and A. Benajiba
Chapter five constitution of Microvillar Enzymes in several stages in their lifestyles Cycles (pages 50–72): Hans Sjostrom, Ove Noren, E. Michael Danielsen and Hanne Skovbjerg
Chapter 6 particular Labelling of the Hydrophobic area of Rat Renal ??Glutamyltransferase (pages 73–91): Thomas Frielle and Norman P. Curthoys
Chapter 7 Biosynthesis and meeting of the biggest and significant Intrinsic Polypeptide of the Small Intestinal Brush Borders (pages 92–112): Giorgio Semenza, Josef Brunner and Hans Wacker
Chapter eight Use of Monoclonal Antibodies within the examine of Intestinal constitution and serve as (pages 113–131): Andrea Quaroni
Chapter nine Biosynthesis and delivery of Plasma Membrane Glycoproteins within the Rat Intestinal Epithelial mobilephone: experiences with Sucrase–Isomaltase (pages 132–163): Hans?Peter Hauri
Chapter 10 Molecular structure of the Microvillus Cytoskeleton (pages 164–179): Anthony Bretscher
Chapter eleven constitution of Human Placental Microvilli (pages 180–194): A. G. sales space and O. A. Vanderpuye
Chapter 12 law of Cytoskeletal constitution and Contractility within the Brush Border (pages 195–215): Mark S. Mooseker, Thomas C. S. Keller and Nobutaka Hirokawa
Chapter thirteen Characterization of Membrane Glycoproteins curious about Attachment of Microfilaments to the Microvillar Membrane (pages 216–232): Evelyne Coudrier, Hubert Reggio and Daniel Louvard
Chapter 14 Structural and sensible dating among the Membrane and the Cytoskeleton in Brush Border Microvilli (pages 233–252): Paul T. Matsudaira
Chapter 15 Conformational alterations within the ??Subunit, and Cation shipping by way of Na+, K+?ATPase (pages 253–272): Peter L. Jorgensen
Chapter sixteen houses of Immunoglobulin G–Fc Receptors from Neonatal Rat Intestinal Brush Borders (pages 273–286): Neil Simister and Anthony R. Rees
Chapter 17 Immunoglobulin G Receptors of Intestinal Brush Borders from Neonatal Rats (pages 287–299): Richard Rodewald, Dorothy Madden Lewis and Jean?Pierre Kraehenbuhl
Chapter 18 Cotransport platforms within the Brush Border Membrane of the Human Placenta (pages 300–326): C. A. R. Boyd
Chapter 19 Chairman's remaining comments (page 327): A. J. Kenny
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Extra info for Ciba Foundation Symposium 95 - Brush Border Membranes
Wucker: But even in the method that uses the iodinated peptide, acid hydrolysis of the isolated hydrophobic anchor is done. Dr Maroux’s interpretation of the membrane anchoring of the peptidase would be more convincing if it did not rely solely on the size of the anchor peptide but provided some independent evidence, say, for the actual location of the N-terminus. Muroux: Are you saying that after acidic hydrolysis it is impossible to do a correct amino acid composition of these peptides? Wucker: It may not be impossible but it may be difficult.
Schmitz: Some of your electron micrographs showed vesicles of natural brush border with only the endopeptidase on it, and another micrograph showed vesicles completely free of protein because of the papain treatment. When you study such natural membranes, are you not able to see those proteins MICROVILLAR ENDOPEPTIDASE 31 as two ranges of knobs, one very near the membrane, which would correspond to endopeptidase, and another one further away? Kenny: The ones further away tend to be the dominant ones.
Huuri: Is anything known about the biosynthesis of enteropeptidase? It is a heterodimer, but do you have any indication that it is synthesized as a singlechain precursor? Hermon-Taylor: We don’t yet know. The structure of enteropeptidase differs between species; in humans the enzyme appears to be a heterotrimer (Magee et a1 1981). We don’t know much about biosynthetic precursor forms but we hope to soon. However, biosynthesis of the enzyme in the high enteropeptidase-secreting proximal small intestine appears to be triggered in response to mediated sodium transport (Bett et a1 1981).