Acta Biologica et Medica Germanica. / Band 36, Heft 11/12, : 3rd Symposium Intracellular Protein Catabolism / / hrsg. von R. Baumann.

• MitwirkendeR: Abramov, Z. T.,; Airhart, J.,; Anachkova, B.,; Ansorge, S.,; Aronson jr., N. N.,; Bakay, R.,; Ballard, F. J.,; Banno, Yoshiko,; Barrett, Alan J.,; Berg, T.,; Betz, H.,; Beynon, Robert J.,; Bielka, H.,; Bird, J. W. C.,; Bohley, P.,; Booth, A. G.,; Bouma, J. M. W.,; Brandenburg, D.,; Brezesinski, G.,; Bruno, M. K.,; Brzin, J.,; Carney, Ian T.,; Chaloupka, J.,; De La Morena, E.,; Dean, Roger T.,; Dron, D. I.,; Dunn, W. A.,; Duursma, A.,; Etherington, D. J.,; Evans, P. J.,; Ferenčik, M.,; Francis, G. L.,; Friedrich, K.,; Giraldi, T.,; Grisolia, S.,; Gruber, M.,; Guba, F.,; Gubenšek, F.,; Hedge, A. M.,; Hermann, V.,; Holzer, H.,; Hood, W.,; Hopgood, M. F.,; Iborra, J.-L.,; Isotova, L. S.,; Jahr, H.,; Jones, R. H.,; Katunuma, Nobuhiko,; Kay, John,; Keilová, H.,; Kenny, A. J.,; Khairallah, E. A.,; Khairallah, L.,; Kirschke, H.,; Knook, D. L.,; Knowles, S. E.,; Kobayashi, Keiko,; Koelsch, R.,; Koenig, H.,; Kohler, E.,; Kohnert, K.-D.,; Kominami, Eiki,; Kooistra, T.,; Kopitar, M.,; Korant, B. D.,; Kotulová, D.,; Kovačič, M.,; Kregar, I.,; Langner, J.,; Lapanje, S.,; Lasch, J.,; Lindigkeit, R.,; Lu, C. Y.,; Macnair, R. D. C.,; Markwardt, F.,; Murgašová, I.,; Mészáros, Magda G.,; Nisi, C.,; Ohkuma, S.,; Papachristodoulou, D.,; Pfeifer, U.,; Philippová, L.,; Pierart-Gallois, M.,; Poole, B.,; Puchalsky, D.,; Reglero, A.,; Richter, V.,; Riemann, S.,; Rivas, J.,; Romer, I.,; Rubio, V.,; Russev, G.,; Römer, I.,; Salama, Z. B.,; Sanada, Yukihiro,; Schmidt, G.,; Schmidt, S.,; Schneider, Y. J.,; Schottelius, B. A.,; Schwartz, W. N.,; Schön, E.,; Seglen, P. O.,; Simon, O.,; Sohár, I.,; Solheim, A. E.,; Spanier, A. M.,; Stanovnik, B.,; Starkey, Phyllis M.,; Stauber, W. T.,; Steiner, D. F.,; Stepanov, V. M.,; Strnadová, M.,; Strongin, A. Ya.,; Stürzebecher, J.,; Suhar, A.,; Sönksen, P. H.,; Takács, Ö.,; Thomas, J. H.,; Tišler, M.,; Tolleshaug, H.,; Tomášek, V.,; Trouet, A.,; Tulkens, P.,; Turk, V.,; Umezawa, Hamao,; Urh, I.,; Walsmann, P.,; Warburton, M. J.,; Welfle, H.,; Wiederanders, B.,; Zühlke, H.,; Čechová, J.,; Štefanovič, J.,
• HerausgeberIn: Baumann, R.,
• Place / Publishing House: Berlin ;, Boston : : De Gruyter, , [2022]; ©1977
• Year of Publication: 2022
• Edition: Reprint 2022
• Language: German
• Series: Acta Biologica et Medica Germanica ; Band 36, Heft 11/12
• Physical Description: 1 online resource (476 p.)

Table of Contents

• Frontmatter
• Preface
• Intracellular proteinase of Bacillus subtilis
• Relationships between intracellular proteolytic activity and protein turnover in Bacillus megaterium
• Characterization and function of intracellular proteinases and proteinase inhibitors from yeast
• Protein degradation during the differentiation of eukaryotic cells : Studies on the sporulation of Saccharomyces cerevisiae and on the formation of the neuromuscular junction in the chick embryo
• Studies on bovine spleen cathepsin D
• Intracellular protein catabolism and new serine proteases
• Cathepsin H: An endoaminopeptidase
• The effect of human neutrophil elastase and cathepsin G on the collagen of cartilage, tendon, and cornea
• The action of cathepsin B and collagenolytic cathepsin in the degradation of collagen
• Protein cleavage in virus-infected cells
• Peptidases of the kidney microvillus membrane
• Degradation of myofibrillar proteins by cathepsins B and D
• Degradation of myones as a consequence of disuse and denervation
• The influence of immobilization on soluble proteins of muscle
• A neutral protease from rat intestinal muscle. A possible role in the degradation of native enzymes
• The susceptibility of glycogen Phosphorylase to inactivation by endogenous and exogenous proteases
• Studies on the possible physiological controls of skeletal muscle proteases
• Lysosomal enzyme secretion in rat ventral prostate. Secretagogue action of testosterone and dibutyryl cyclic AMP
• Evidence pointing to the main role of lysosomes in mitochondrial proteolysis at neutral pH
• Increased susceptibility of carbamylated glutamate dehydrogenase to proteolysis
• Acetyl glutamate — a model of signals for intracellular proteolysis
• Flow and shuttle of plasma membrane during endocytosis
• Inhibition by insulin of the physiological autophagic breakdown of cell organelles
• Proteolytic and transhydrogenolytic activities in isolated pancreatic islets of rats
• Studies on the relationship between the molecular structure and the catabolism of insulin
• Insulin and glucagon degradation in livers of sand rats (Psammomys obesus)
• Conversion of proinsulin into insulin by cathepsins B and L from rat liver lysosomes
• Presence of an endopeptidase activity in rat liver ribosomes
• Implications of amino acid compartmentation for the determination of rates of protein catabolism in livers in meal fed rats
• The role of lysosomal enzymes in protein degradation in different types of rat liver cells
• Uptake and degradation of asialo-fetuin by isolated rat hepatocytes
• Endocytosis and breakdown of proteins by sinusoidal liver cells
• The accumulation of weakly basic substances in lysosomes and the inhibition of intracellular protein degradation
• Protein degradation in isolated rat hepatocytes
• Attempts to relate enzyme inactivation to degradation in vivo
• Lysosomes and protein degradation
• Protein degradation in rat liver cells
• Intracellular protein catabolism
• Pepstatin- and leupeptin-loaded liposomes: A tool in protein breakdown studies
• Turnover of lipogenic enzymes of rat liver in dependence on age
• Aging changes in intracellular protein breakdown
• Cooperation of various subcellular fractions in protein degradation in vitro
• Pharmacological control of hyperproteolytic states in blood by enzyme inhibitors
• Biochemical and biological properties of cell and tissue neutral proteinases and inhibitors
• Naturally occurring inhibitors of intracellular proteinases
• Isolation and characterization of inhibitors of neutral proteinases from spleen
• Production of rabbit antibodies against active rat cathepsin B
• Role of heparin in the interaction of serine proteinases with antithrombin III
• Protease inhibitors produced by microorganisms
• Inhibition of glycoprotein catabolism in vivo and in the perfused rat liver
• Studies on the in vivo-action of leupeptin on the nitrogen retention in rats
• Inactivation studies of cathepsin D with diazo compounds
• Inhibition of serine proteinases by benzamidine derivatives
• Studies on some effectors of lysosomal proteinases from rat liver
• Endogenous proteolytic activity of chromatin
• Degradation of phosphorylated chromosomal nonhistone proteins
• Interaction of intracellular proteases and immune mechanisms
• The diversity of cellular proteinases in physiology and pathology
• CONTENTS/ СОДЕРЖАНИЕ/ INHALT