Single gene comparisons

Figure 1-7-8. Comparison of Probes Single-Gene Versus Allele-Specific Oligonucleotide (ASO)...

Figure 5.7. There are many examples now known of the synthesis of NPs via matrix pathways (see also Figure 9.3). However, a nice example of the benefit of such flexibility was revealed when a mutant of spearmint that had smelled more like peppermint was studied.A comparison of the terpenes in both plants revealed that the single gene mutation had not resulted in a single chemical change but multiple changes, in the mutant plant, a hydroxyl group was added to the 3-position of the cyclohexene ring of limonene while the wild-type hydroxylated the 6-position. Some of the other wild-type tailoring enzymes in the mutant did not discriminate fully between the 3- and 6-hydroxylated products so a new family of NPs were produced which gave the mutant plant an odour of peppermint.

The bird lysozymes c, of which chicken egg white lysozyme (CL) is the most extensively studied example, provide an ideal system to recreate evolutionary intermediates and to study structure-function relationships of reconstructed ancestral proteins. Three major considerations qualify the avian lysozyme system for reconstruction of evolutionary pathways (1) the biochemistry of the enzymes has been extensively studied and well characterized,3,4 (2) there are many natural variants available from other birds, and homologous comparisons can be ensured since lysozymes for all game birds are encoded by a single gene,5 and (3) the three-dimensional structure of CL has been resolved at the atomic level, which allows for structural interpretation of the mutational impact.2,4 Proteins representing the ancestral, evolutionarily intermediate, and derived states of chicken and related bird lysozymes are made and characterized as described below. 

Condie, A., Ecles, R., Bprresen, A.-L., Coles, C., Cooper, C., and Prosser, J. (1993) Detection of point mutations in the p53 gene comparison of single-strand conformation polymorphism, constant denaturant gel electrophoresis, and hydroxylamine and osmium tetroxide techniques. Human Mutat. 2, 58-66. 

STR was first purified by Treimer and Zenk [78, 79] and Mizukami et al. [80] from cell cultures of C. roseus. The enzyme was found to have a high substrate specificity, and to suffer no inhibition by end-product alkaloids, such as vindoline and catharanthine [78-80]. It was observed that STR occurred as different isoenzymes [81, 82], and the subcellular localization was determined to be the vacuole [83]. The complete mRNA sequence of Str was determined by Pasquali et al. [84], who also showed that STR is encoded by a single-copy gene, indicating that the above mentioned isoenzymes are formed post-translationally from a single precursor. Comparison of the primary structure of the STR protein with the amino acid sequence deduced from the Str mRNA showed the... 

In contrast to TIM, which is not available as a single gene product. PGK is expressed both as bifunctional PGK-TIM fusion protein and as separate monomeric entity. The comparison of the physicochemical data for both forms... 

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