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The Global ETD Search service is a free service for researchers
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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 11 to 20 of 260 (0.029 seconds)Spelling suggestions: "subject:"pela."" "subject:"peak.""
| 11 |
Structural characterisation of photosystem IISharma, Jyoti January 1995 (has links)
Protocols were developed to fractionate each of the five protein components present in the PSII reaction centre complex, isolated from the thylakoid membrane of pea plants. The precise molecular weights of all the purified components were then successfully determined, for the first time by electrospray and fast atom bombardment mass spectrometry. Discrepancies between the molecular weights assigned and those calculated from the respective cDNA sequences were observed for all of the reaction centre component proteins. Application of novel mapping and sequencing strategies on these proteins has assured the elucidation of full primary structures of and subunits of cytochrome b559 and the majority of the structures of the D1 and D2 proteins. In the case of the subunit to cytochrome b559 an N-terminal processing event, involving the removal of the initiating formyl-methionine residue was found. The transformations on the subunit of cytochrome b559 were characterised as a N-terminal modification, entailing the processing of the formyl-methionine residue followed by an acetylation of the amino terminus of the mature protein, and a sequence change at residue twenty six, were a serine has been replaced by a phenylalanine residue. This was presumed to be due to an error in the gene sequence, but is more probably a result of the recently described phenomenon of mRNA editing. Currently, the nucleotide sequence of the pshI gene from pea plants is not available. Using a combination of mass spectrometric techniques and automated gas phase sequencing the primary structure of this component has been obtained in these studies. In contrast to the smaller subunits, data obtained on the D1 and D2 proteins indicated that both these components exist in heterogeneous forms. Mapping studies on these subunits have identified phosphorylation and oxidation, as at least two sources of this microheterogeneity.
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| 12 |
Evolution of resistance to natural enemiesFerrari, Julia January 2001 (has links)
No description available.
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| 13 |
Digestion and large intestinal fermentation of pea (Pisum sativum) carbohydratesGoodlad, J. S. January 1989 (has links)
No description available.
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| 14 |
An investigation of the gibberellins of Pisum sativum LDavies, J. K. January 1984 (has links)
No description available.
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| 15 |
The effect of the r locus on the synthesis of storage proteins in Pisum sativumTurner, S. R. January 1988 (has links)
No description available.
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| 16 |
In situ hybridisation for studying embryo development in Pisum sativum LHauxwell, Angela Jane January 1990 (has links)
No description available.
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| 17 |
Promotion and prevention of infection thread development in the Rhizobium-legume symbiosisGardner, Chris January 1996 (has links)
No description available.
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| 18 |
The resistance of Pisum to Mycosphaerella pinodes (Berk. and Blox.) VestergrClulow, Stephen A. January 1989 (has links)
No description available.
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| 19 |
The rug-3 locus of peaHarrison, Christopher John January 1996 (has links)
No description available.
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| 20 |
In vitro protein digestibility : a comparison of seeds from near isogenic pea lines and the role of trypsin inhibitorsAl-Wesali, Mohammad Saad January 1995 (has links)
No description available.
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