Download Advances in Post-Translational Modifications of Proteins and by Soo I. Chung, Sung Keun Chang, Enzo T. Cocuzzi, J. E. Folk, PDF

By Soo I. Chung, Sung Keun Chang, Enzo T. Cocuzzi, J. E. Folk, Hee Chul Kim, Soo Young Lee (auth.), Vincenzo Zappia, Patrizia Galletti, Raffaele Porta, Finn Wold (eds.)

ISBN-10: 1468490443

ISBN-13: 9781468490442

This quantity comprises fifty six contributions offered on the 1st overseas Symposium on Post-Translational differences of Proteins and growing older, hung on the Island of Ischia (Naples, Italy) from could eleven to fifteen, 1987, less than the auspices of the college of Naples and the Italian Society of Biochemistry. the first objective of this interdisciplinary assembly was once to advertise a efficient alternate between scientists from various cultural parts, and to provide them the chance to debate difficulties of universal curiosity approached from diversified medical standpoints. even if loads of reports has resulted in a definition of the chemical mechanisms and of the most enzymological facets of the various post-translational adjustments of proteins, we're nonetheless far-off from an entire elucidation of the practical importance of such techniques. in actual fact, it sort of feels average that the shortly to be had experi­ psychological techniques and versions hired to enquire the organic roles are nonetheless insufficient. the hunt for compatible version structures used to be a question of debate through the assembly, and should be an enormous problem sooner or later. the main usually hired techniques to this challenge so far were in vitro, yet numerous proteins said to be first-class in vitro substrates didn't express any task while assayed in in vivo models.

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Extra resources for Advances in Post-Translational Modifications of Proteins and Aging

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W•• Ichinose. A•• and Leytus. S. P •• 1986. Structural features of the proteins participating in blood coagulation and fibrinolysis. Cold Spring Harbor Symp. Quant. BioI •• 51:509-514. Duckert. F •• 1972. Documentation of the plasma factor XIII deficiency in man. Ann. Y. Acad. Sci •• 202:190-199. Emori. , Kawasaki. H•• Sugihara. H•• lmajoh. S •• Kawashima. S •• and Suzuki. K•• 1986. Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease.

EXTRACELLULAR FACTOR XIII, A2B2 The liver has been suggested as the site of synthesis of extracellular or plasma FXIII. I ,23-2s Previous evidence based on clinical data documents reduced levels of plasma FXIII in association with liver disease in some patients but not in others; but, in fact, a decrease in plasma FXIII correlates with the severity of the systemic disease rather than with any specific illness. To address the question of the site of synthesis of plasma . 26-35 FXIII, a well-characterlzed human hepatoma cell line, Hep G2, was selected as a prototype of hepatocytes and used to investigate FXIII biosynthesis.

35:1487. Schwartz, M. , Pizzo, S. , Hill, R. , and McKee, P. , 1973, Human factor XIII from plasma and platelets, J. BioI. , 248:1395-1407. Shen, L. , McDonagh, R. , 1975, Effects of calcium ion and covalent cross1inking on formation and elasticity of fibrin gels, Thromb. , 6:255-265. , 1983, Contribution of fibrin stabilization to clot strength, J. C1in. , 71:1336-1341. Sixma, J. , Gueze, H. , 1984, Immunocytochemical localization of albumin and factor XIII in thin cryo sections of human blood platelets, Thromb.

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