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The Global ETD Search service is a free service for researchers
to find electronic theses and dissertations. This service is
provided by the
Networked Digital Library of Theses and Dissertations.
Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
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Showing 311 to 320 of 16178 (0.109 seconds)Spelling suggestions: "subject:"probeprotein"" "subject:"proprotein""
| 311 |
Evaluation of PKC isozyme expression, overexpression and antinsense-suppression in C6 glioma cells and primary articular chondrocytesBeale, Gary S. January 1999 (has links)
No description available.
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| 312 |
Studies on the cell-free synthesis of the myelin basic proteinJenner, S. A. January 1984 (has links)
No description available.
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| 313 |
Regulation and functional aspects of Xenopus BrachyuryLerchner, Walter January 1999 (has links)
No description available.
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| 314 |
The accumulation of proteins in the Xenopus oocyte nucleusDingwall, C. January 1985 (has links)
The ability of proteins to accumulate in the nucleus has been studied by injecting nucleoplasmin and calf thymus histone H1 into the cytoplasm of Xenopus oocytes. Nucleoplasmin, the most abundant protein in the Xenopus oocyte nucleus is pentameric and proteolysis of the nuceloplasmin pentamer produces a relatively protease resistant 'core' molecule that cannot enter the nucleus after microinjection into the cytoplasm. The polypeptide domain ('lq tail') of each subunit removed by proteolysis was obtained as a discrete fragment and has the ability to accumulate in the nucleus. Partially cleaved pentameric molecules with a single intact sub unit can still accumulate in the nucleus. Therefore a polypeptide domain of nucleoplasmin has been found that is both necessary and sufficient for accumulation in the nucleus. When the `core' molecule was injected directly into the oocyte nucleus it remained there, indicating that the 'tail' region confers selective entry rather than selective retention. In the case of histone H1 a proteolytic fragment encompassing the carboxyterminal domain can accumulate in the nucleus. The amino acids lysine, proline and alanine comprise 75 of the 89 amino acids in this fragment. Since the remaining 14 amino acids are scattered throughout the fragment and not clustered any primary sequence specifying entry into the nucleus would seem necessarily to involve the amino acids lysine, proline and alanine. Positive charge alone cannot explain the accumulation of this gragment since poly L-lysine does not accumulate after microinjection into the cytoplasm. Fragments encompassing other domains of the molecule are so unstable in the oocyte that their ability to accumulate in the oocyte nucleus cannot be assayed. The gene for nucleoplasmin has been cloned and sequences have been found in the 'tail' region of nuceloplasmin that show homology to sequences identified in other nuclear proteins that appear to constitute a signal specifying nuclear localisation.
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| 315 |
Influence of insulin and glucagon on protein metabolism and resting metabolic ratePacy, P. J. H. January 1988 (has links)
No description available.
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| 316 |
The accuracy of foreign protein translation by Escherichia coliScorer, Carol Amanda January 1989 (has links)
No description available.
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| 317 |
Structural and immunological characterisation of FIM D, a minor fibrial protein of Bordetella pertussisMatheson, Mary Ann January 1996 (has links)
No description available.
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| 318 |
The aqueous photochemistry of small peptidesBirch, D. January 1986 (has links)
No description available.
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| 319 |
Chemical modification of streptavidinHolding, Finn Peter January 1994 (has links)
No description available.
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| 320 |
A mechanistic study of the molecular chaperone GroELGray, Tamara Eve January 1993 (has links)
No description available.
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