Cysteine Proteinases and their Inhibitors: Proceedings of the International Symposium Portoroz, Yugoslavia, September 15–18, 1985

دانلود کتاب Cysteine Proteinases and their Inhibitors: Proceedings of the International Symposium Portoroz, Yugoslavia, September 15–18, 1985

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کتاب سیستئین پروتئین ها و مهارکننده های آن: مجموعه مقالات سمپوزیوم بین المللی پورتوروز، یوگسلاوی، 15 تا 18 سپتامبر 1985 نسخه زبان اصلی

دانلود کتاب سیستئین پروتئین ها و مهارکننده های آن: مجموعه مقالات سمپوزیوم بین المللی پورتوروز، یوگسلاوی، 15 تا 18 سپتامبر 1985 بعد از پرداخت مقدور خواهد بود
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توضیحاتی در مورد کتاب Cysteine Proteinases and their Inhibitors: Proceedings of the International Symposium Portoroz, Yugoslavia, September 15–18, 1985

نام کتاب : Cysteine Proteinases and their Inhibitors: Proceedings of the International Symposium Portoroz, Yugoslavia, September 15–18, 1985
عنوان ترجمه شده به فارسی : سیستئین پروتئین ها و مهارکننده های آن: مجموعه مقالات سمپوزیوم بین المللی پورتوروز، یوگسلاوی، 15 تا 18 سپتامبر 1985
سری :
نویسندگان :
ناشر : De Gruyter
سال نشر : 1986
تعداد صفحات : 864
ISBN (شابک) : 9783110846836 , 9783110107241
زبان کتاب : English
فرمت کتاب : pdf
حجم کتاب : 46 مگابایت



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فهرست مطالب :


PREFACE\nACKNOWLEDGEMENT\nORGANIZING COMMITTEE\nCONTENTS\nNOMENCLATURE AND CLASSIFICATION OF THE PROTEINS HOMOLOGOUS WITH THE CYSTEINE PROTEINASE INHIBITOR CHICKEN CYSTATIN\nGENERAL CYSTEINE PROTEINASES\nIsolation, properties , primary structure and cloning\nHuman cathepsins B, H and L: characterization by amino acid sequences and some kinetics of inhibition by the kininogens\nTentative amino acid sequence of bovine spleen cathepsin B\nInhibition of human liver cathepsins B, H and L by the human α2 cysteine proteinase inhibitor\nHuman kidney cathepsin L\nLatent human cathepsin L\nCloning of a bovine protein homologous with cysteine proteinases and identification of the gene\nImmunological studies on the secreted forms of cathepsin B\nA study of the peptidyldipeptidase activity of bovine spleen cathepsin B using synthetic substrates\nComparison of characteristics and drug-induced modifications of rat spleen cathepsins B and H\nCystein proteinase activities in embryonic chicken sekeletal muscle\nHistone degradation by lysosomal proteases\nProperties of a cysteine proteinase from human thyroids\nPrimary structure and function of calcium activated neutralprotease\nIdentification of two alkaline cysteine proteinases from rat skeletal muscle\nMultiple forms, structure and specificity of clostripain\nEnzymatic and immunological identification of a cysteine proteinase procoagulant in human melanoma\nThyroid cysteine proteinases that catalyze release of thyroxine from thyroglobulin and thyroxine-containing peptide\nProteases in African trypanosomes\nCharacterization of a cysteinyl proteinase from the human parasite, Schistosoma mansoni\nStudies on a proteinase inactivating enzyme from the basidiomycete Coprinus atramentarius\nGENERAL CYSTEINE PROTEINASES OF DIFFERENT ORIGIN\nLocalization and biological role\nDistributions and localizations of lysosomal cysteine proteinases and cystatins\nFunctional shares of cathepsins B, H and L in autophagy and heterophagy\nPost mortem localization of lysosomal peptide hydrolase, cathepsin B\nBifunctional derivatives of L-trans-epoxysuccinyl-L- -leucylamido-(4-amino)butane (Ep-459) as potential localization agents for cysteine proteinases\nCysteine proteinases and bone resorption\nThe role of collagen-degrading cysteine proteinases in connective tissue metabolism\nThe role of cathepsins H and B, and inhibitors leupeptin and CPI in proliferative activities of non-malignant cells in culture\nViruses as vectors for cysteine proteases\nMECHANISM OF ACTION OF CYSTEINE PROTEINASES\nNatural structural variation in the cysteine proteinases as an aid to the study of mechanism by reactivity probe kinetics, catalysis kinetics and spectroscopic methods\nMechanism of action of cysteine proteases: 1/ differences from serine enzymes;2/ the second thiol group of chymopapain\nProposal of the double regulation mechanism for the action of calpain\nControl mechanism of calcium-activated neutral protease (CANP) activity\nGENERAL CYSTEINE PROTEINASE INHIBITORS\nIsolation, properties and primary structure\nThe mammalian cysteine proteinase inhibitors. Structural diversity and evolutionary origin\nKininogens as thiol proteinase inhibitors\nCystatin-like domains of LMW-kininogen, and speculations on the evolution of cystatins\nHuman stefins and cystatins: their properties and structural relationships\nIsolation of kininogens using affinity chromatography\nCharacterization of low molecular mass cysteine proteinase inhibitors from human amniotic fluid\nProperties and structure of human spleen stefin B - a low molecular weight protein inhibitor of cysteine proteinases\nAmino acid sequence of the cysteine proteinase inhibitor cystatin B from human liver\nCystatin S and the related cysteine proteinase inhibitors in human saliva\nCystatin C (Post γ Globulin) in serum from patients with autoimmune diseases\nDifferential actions of human cystatin C on different functions of granulocytes\nPotentiation of excretion of canine cystatin-C (Post-gamma globulin)\nThe 43 kDa papain inhibitor in human tissues\nSmall and high molecular weight proteinase inhibitors from bovine muscle\nLow molecular weight protein inhibitors of cysteine proteinases from bovine parotid glands\nThe interaction of papain molecule with thiol proteinase inhibitors from newborn rat epidermis\nChicken egg white cystatin as a ligand for affinity chromatography\nDistribution of the egg white cystatin in chicken\nIsolation and characterization of chicken egg white low-Mr kininogen\nPapain inhibition by snake venoms\nCysteine proteinase inhibitors from fish liver\nCysteine proteinase inhibitors from sea anemone\nCharacterization of low molecular weight and high molecular weight endogenous inhibitors of calcium activated neutral protease\nCalpain inhibition by peptide epoxides and the effect of autolysis\nEST, a new analog of E-64, can prolong the life span of dystrophic hamsters, UM-X7.1\nGENERAL CYSTEINE PROTEINASE INHIBITORS\nLocalization, biological function and kinetics\nCystatins A and B in normal and pathologically altered human tissues\nChicken and rat muscle cystatins and their localization in cultured myoblasts\nDistribution and solubilization of a high molecular weight cysteine proteinase inhibitor from rat epidermis\nPossible biological functions of protein proteinase inhibitors\nA curve-fitting approach to the determination of kinetic constants of proteinase inhibitors\nInhibition of cathepsins B, H and L by rat thiostatin, the circulating α1 cysteine proteinase inhibitor, and by an active fragment\nCYSTEINE PROTEINASES AND THEIR INHIBITORS IN TUMORS\nTumor cysteine proteinases and their inhibitors\nThiol protease inhibitor released from human malignant melanoma\nPROTEINASES AND THEIR INHIBITORS\nMedical aspects\nCystatin C (α-trace) amyloidosis\nSome biochemical aspects of chymopapain treatment of sciatica\nGranulocyte proteinases as mediators of unspecific proteolysis in inflammation: a review\nLIST OF PARTICIPANTS\nAUTHOR INDEX\nSUBJECT INDEX




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