By Brian Henderson, A. Graham Pockley

This booklet stories knowing of the organic roles of extracellular molecular chaperones. It presents an outline of the constitution and serve as of molecular chaperones, their function within the mobile reaction to emphasize and their disposition in the mobile. It additionally questions the fundamental paradigm of molecular chaperone biology - that those proteins are at first protein-folding molecules. Paradigms of protein secretion are reviewed and the evolving idea of proteins (such as molecular chaperones) as multi-functional molecules for which the time period 'moonlighting proteins' has been brought is mentioned. The function of exogenous molecular chaperones as phone regulators is tested and the physiological and pathophysiological function that molecular chaperones play is defined. within the ultimate part, the aptitude healing use of molecular chaperones is defined and the ultimate bankruptcy asks the query - what does the long run carry for the extracellular biology of molecular chaperones?

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C. A. Bardwell, and T. E. Creighton, Biochemist~v 32, 5083 (1993). ~ M. Wunderlich, R. Jaenicke, and R. Glockshuber. J. Mol. Biol. 233, 559 (1993). 57 A. Holmgren, Methods EnzymoL 107, 295 (1984). ~s H. F. Gilbert, Biochemistry 28, 7298 (1989). s,~ N. J. Darby. R. B. Freedman, and T. E. Creighton, Biochemistry 33, 7937 (1994). ,{i T. E. Creighton, Science 256, l l l (1992). (,i j. S. Weissman and P. S. Kim, Science 256, 112 (1992). [3] PROTEIN DISULFIDE ISOMERASE 43 large number of intermediates with normative disulfide pairings and with mixed disulfides between the protein and the glutathione redox buffer,62 64 and the rearrangement of these nonnative disulfides often limits the rate of the overall process.

Chem. Stand. 7, 1129 (1953). /4 C. Ma, W. Kudlicki, O. W. Odom, G. Kramer. and B. Hardesty, Biochemist O, 32, 7939 (1993). is D. Baccanari, A. Phillips, S. Smith, D. Sinski, and J. Burchall, Biochemist O, 14, 5267 (1975). i(, M. J. Sleigh, Anal. Biochem. 156, 251 (1986). 26 MOLECULARCHAPERONES [31 the amount of enzyme that produces i/xmol of acetylated chloramphenicol per minute at 30 °. Comments In the chaperone-deficient E. coli A19 system described here, using salt-washed ribosomes and the late-eluting fractions after Sephadex G-150 chromatography of the p-r fraction, the GroEL concentration is reduced to approximately 10% of the value determined for the coupled transcription/ translation system with the $30 fraction.

Because the cCMP concentration is near the Km and the product, CMP, is a competitive inhibitor of RNase, the observed velocity of cCMP hydrolysis depends not only on the concentration of active RNase, but also on the concentrations of the substrate (cCMP) and product (CMP). The depletion of cCMP and the inhibition by the product mean that the same molar amount of active RNase will generate a larger absorbance change during the initial part of the assay than in the final stages of the assay. The procedure for determining the amount of active RNase at any time amounts to calculating the concentration of fully active RNase that would 37 S.

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