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 specific Topological good points 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 most important 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 shipping of Plasma Membrane Glycoproteins within the Rat Intestinal Epithelial phone: reviews 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 all for Attachment of Microfilaments to the Microvillar Membrane (pages 216–232): Evelyne Coudrier, Hubert Reggio and Daniel Louvard
Chapter 14 Structural and sensible courting among the Membrane and the Cytoskeleton in Brush Border Microvilli (pages 233–252): Paul T. Matsudaira
Chapter 15 Conformational adjustments within the ??Subunit, and Cation delivery by way of Na+, K+?ATPase (pages 253–272): Peter L. Jorgensen
Chapter sixteen homes 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 remaining feedback (page 327): A. J. Kenny
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Extra info for Ciba Foundation Symposium 95 - Brush Border Membranes
Purification and molecular properties. Biochim Biophys Acta 599:448-463 Feracci H, Bernadac A, Gorvel JP. Maroux S 1982a Localization by immunofluorescence and histochemical labeling of aminopeptidase N in relation to its biosynthesis in rabbit and pig enterocytes. Gastroenterology 82:317-324 Feracci H, Maroux S, Bonicel J , Desnuelle P 1982b The amino acid sequence of the hydrophobic anchor of rabbit intestinal brush border aminopeptidase N . Biochim Biophys Acta 684:133-136 Forbush B, Kaplan JH, Hoffman JF i978 Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and a proteolipid component of Na,K-ATPase.
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. You might easily lose, say, dipeptides during the hydrolysis and the consequent compositional analysis. Muroux: During the amino acid analysis, if peptide hydrolysis was not complete, the resulting peptides did not elute at the same positions at which the amino acids were recovered on the column. Smith: You speculated, Dr Maroux, that the free peptides associated or unassociated with aminopeptidase may be concerned with amino acid movement across the brush border membrane.
This gives a yield of 100% for this paminopeptidase whereas the detergent form and peptide are bound. Thus, x can be calculated. This value enables the amino acid analysis to be interpreted in terms of the number of residues per mole and, hence, the relative molecular mass of the peptide can be computed. For a dimeric enzyme, 2 X y moles of peptide can be liberated per mole of aminopeptidase, thus leading to a dilution factor of (x + 2y)/x. This is true for pig aminopeptidases N and A, assuming that the anchor peptides of these enzymes have the same relative molecular masses as the anchor peptide of rabbit aminopeptidase, which is strongly suggested by analysis on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate (SDS) (Benajiba & Maroux 1980, 1981).
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