Chapter 1 Chairman's creation (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 precise 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 existence 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 telephone: stories 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 rules 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 interested in Attachment of Microfilaments to the Microvillar Membrane (pages 216–232): Evelyne Coudrier, Hubert Reggio and Daniel Louvard
Chapter 14 Structural and practical 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 means 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 structures within the Brush Border Membrane of the Human Placenta (pages 300–326): C. A. R. Boyd
Chapter 19 Chairman's last feedback (page 327): A. J. Kenny
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Extra resources for Brush border membranes. Ciba Foundation symposium 95
4a rather than those in Fig. 4b. They may therefore represent stalked proteins like the endopeptidase, which are not released by papain. It is tempting to extend the argument to suggest that different populations of microvilli exist, some bearing papain-sensitive and others bearing papainresistant stalks, but this has yet to be investigated. Thus, we can propose a simple structural explanation for the inability of proteinases to release the endopeptidase from the membrane. It is not because the endopeptidase is deeply imbedded in the membrane but, rather, because it belongs to another class of stalked protein in which the stalk is shorter than most, thereby hindering access to the stalk by trypsin or papain.
It is supposed in Fig. 3 that non-sequenced hydrophobic residues remaining in the anchor peptide that is released by trypsin could complete this hydrophobic sequence by crossing the lipid bilayer. The hydrophilic residues could be located, on the other hand, in a region following + + + 40 MAROUX ET AL this hydrophobic core, and could emerge from the membrane on the luminal side. 2, GLXI, PRO, HIS, LYS, pae9000 AGE - ASN-THR-X- GLN- SER-PRO-X-MET-ALA-X-X-ASN-X-X- 40 AMINO SUGARS 60 NEUTRAL SUGARS FIG.
The continuous lines show the effect of the anti-endopeptidase serum. Not shown is the effect of the antiserum on the phosphoramidon-insensitive activity-no inhibition was observed in any of the three tissues. peptide bonds of hydrophobic residues) makes it generally useful in degrading many different biologically active peptides. Its roles in limiting the activity of various peptide hormones or neurotransmitters may depend on its precise cellular location rather than on its specificity for a particular substrate.