By Paul Eggleton, Marek Michalak (auth.), Paul Eggleton Ph.D., Marek Michalak Ph.D. (eds.)
The e-book specializes in the newest discoveries on calreticulin, calnexin and different endoplasmic reticulum proteins. Calreticulin has been implicated to impact various mobile functionality and play a task in lots of pathologies together with protein folding issues, cardiac pathologies, melanoma and autoimmunity. This ebook includes contributions from the realm leaders within the sector of endoplasmic reticulum functionality, protein folding, Calcium homeostasis and autoimmunity. It increases many fascinating questions on calreticulin, calnexin and the endoplasmic reticulum and offers a special chance to gain the importance of those calcium-binding chaperones. The publication is exclusive in each admire and we aren't conscious of the other e-book targeting those facets of endoplasmic reticulum biology. as a result of a vital position of endoplasmic reticulum, calreticulin and calnexin in almost all mobile services, the booklet might be of curiosity to every person within the organic sciences.
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Additional info for Calreticulin: Second Edition
Bouvier and Stafford3 ! and Hejrup et al23 demonstrated that limited proteolysis of human calreticulin produced a stable fragment with only the C-terminal acidic residues (340-400) cleaved off. Significantly, a fragment consisting of residues 1-337 of rat calreticulin retains rhe chaperoning ability of full-length CRT. 38 Hejrup et al found that the addition of any ofCaCIz, MgCIz, ZnClz, EDTA or EGTA to the reaction increased the rate of proteolysis, which they ascribed to the effects of these molecules on the proteinase K used in the digests .
44. Zapun A, Perrescu SM, Rudd PM et aI. Conformar ion-independenr binding of monoglucosylared ribonucl ease B ro calnexin. Cell 1997; 88(1):29-38. 45. Oliver JD , Roder ick HL, Llewellyn DH er al. ERp57 funcrions as a subunir of specific complexes formed wirh rhe ER lecrins calrericulin and calnexin. Mol Bioi Cell 1999; 10(8):2573-2582 . 46. Frand AR, Kaiser CA. Erol p oxidizes prorein disulfide isomerase in a parhway for disulfide bond formarion in rhe endoplasmic rericulum. Mol Cell 1999; 4(4):469-4 77.
29 The far-UV spectrum demonstrated a strong minimum at 208 nm and a shallow minimum at 226 nm . f" This result is in agreement with the predictions of 12 Co/reticulin calreticulin's secondary structure with , the N-domain predicted to be predominantly /3-sheet and the C-domain consisting of a-helices. Provencher-Glockner secondary structure calculations based on the CD spectra indicate that calreticulin contains 10 % a-helix, 37 % /3-sheet and 29 % /3-turn. Gel filtration chromatography analysis of calreticulin has surprisingly revealed that the protein elutes at a position corresponding to a significantly larger size than its calculated Mw (46,500).