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  • About
  • 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.
311

Evaluation of PKC isozyme expression, overexpression and antinsense-suppression in C6 glioma cells and primary articular chondrocytes

Beale, Gary S. January 1999 (has links)
No description available.
312

Studies on the cell-free synthesis of the myelin basic protein

Jenner, S. A. January 1984 (has links)
No description available.
313

Regulation and functional aspects of Xenopus Brachyury

Lerchner, Walter January 1999 (has links)
No description available.
314

The accumulation of proteins in the Xenopus oocyte nucleus

Dingwall, 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.
315

Influence of insulin and glucagon on protein metabolism and resting metabolic rate

Pacy, P. J. H. January 1988 (has links)
No description available.
316

The accuracy of foreign protein translation by Escherichia coli

Scorer, Carol Amanda January 1989 (has links)
No description available.
317

Structural and immunological characterisation of FIM D, a minor fibrial protein of Bordetella pertussis

Matheson, Mary Ann January 1996 (has links)
No description available.
318

The aqueous photochemistry of small peptides

Birch, D. January 1986 (has links)
No description available.
319

Chemical modification of streptavidin

Holding, Finn Peter January 1994 (has links)
No description available.
320

A mechanistic study of the molecular chaperone GroEL

Gray, Tamara Eve January 1993 (has links)
No description available.

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