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

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.)

This quantity comprises fifty six contributions provided on the 1st foreign Symposium on Post-Translational variations of Proteins and getting old, hung on the Island of Ischia (Naples, Italy) from may well eleven to fifteen, 1987, lower than the auspices of the collage of Naples and the Italian Society of Biochemistry. the first goal of this interdisciplinary assembly was once to advertise a efficient alternate between scientists from diverse cultural parts, and to offer them the chance to debate difficulties of universal curiosity approached from diverse clinical standpoints. even if numerous stories has resulted in a definition of the chemical mechanisms and of the most enzymological features of different post-translational changes of proteins, we're nonetheless distant from an entire elucidation of the sensible value of such techniques. in reality, it sort of feels moderate that the shortly to be had experi­ psychological methods and versions hired to enquire the organic roles are nonetheless insufficient. the hunt for compatible version structures used to be an issue of debate in the course of the assembly, and should be an enormous problem sooner or later. the main often hired techniques to this challenge to date were in vitro, yet numerous proteins suggested to be first-class in vitro substrates did not express any task while assayed in in vivo models.

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Nine out of the 14 proteins with GP-I structures are involved in the complement system, and 5 are involved in diverse systems such as blood coagulation, lymphocyte activation, or oxygen transport. The 1st structure at the top of Fig. 5 represents the protein assembled only by GP-I structures. Beta 2-glycoprotein I, protein H, the b subunit of factor XIII, and C4 binding protein are included in this type. In haptoglobin, the 1st Cys forms an intermolecular disulfide bridge, since the 3rd Cys residue is lost.

In each case, the Coomassie staining pattern and the corresponding autoradiogram showed single immunoprecipitation arcs with identical mobility and area. Figure 9 shows that the radiolabeled FXIII present in the culture medium or extracted by Triton X-lOO from the cell layer comigrated with the FXIII in human plasma or with purified FXIII A2B2 , indicating both electrophoretic and antigenic identity. These results imply that the intrinsically labeled FXIII was identical to the plasma FXIII molecule.

No inhibition of binding by the Rep G2 SFCM was detectable until the SFCM had been concentrated approximately 100-fold. Approximately 15% inhibition was detected with 120-fold concentrated Hep G2 SFCM. The level of FXIII in the Hep G2 SFCM, even when concentrated 120fold, was not sufficient to achieve complete (100%) inhibition in either assay. Mathematical analysis of the data in Figures 6A and 6B suggests that the slopes of the linear portions of the sigmoidal binding curves are parallel to each other, indicating that the antigenic determinants recognized by the antisera are the same in the FXIII found in the Hep G2 SFCM as in the purified FXIII molecules.

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