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Biomedical subjects

Geoff Wilson

Publications and source records attributed to Geoff Wilson.

5 recordsLinked to original sources
PubMed2005

The experience of males entering Nursing: a phenomenological analysis of professionally enhancing factors and barriers.

Males in nursing undoubtedly represent a minority group. However there have been relatively few studies which have investigated their unique experiences, compared with women in male dominated professions. This study conducted in an undergraduate nursing program, analysed the experience of males in nursing regarding (1) decision to enter the profession, during the course, both academic and clinical and (2) methods appropriate for recruiting more males to the profession. In general the results indicate overall positive acceptance of males in nursing, but several factors explored, indicate that change is essential if males are to remain and flourish in the profession.

Adult↗
PubMed2003

Purification and characterisation of a novel DNA methyltransferase, M.AhdI.

We have cloned the M and S genes of the restriction-modification (R-M) system AhdI and have purified the resulting methyltransferase to homogeneity. M.AhdI is found to form a 170 kDa tetrameric enzyme having a subunit stoichiometry M2S2 (where the M and S subunits are responsible for methylation and DNA sequence specificity, respectively). Sedimentation equilibrium experiments show that the tetrameric enzyme dissociates to form a heterodimer at low concentration, with K(d) approximately 2 microM. The intact (tetrameric) enzyme binds specifically to a 30 bp DNA duplex containing the AhdI recognition sequence GACN5GTC with high affinity (K(d) approximately 50 nM), but at low enzyme concentration the DNA binding activity is governed by the dissociation of the tetramer into dimers, leading to a sigmoidal DNA binding curve. In contrast, only non-specific binding is observed if the duplex lacks the recognition sequence. Methylation activity of the purified enzyme was assessed by its ability to prevent restriction by the cognate endonuclease. The subunit structure of the M.AhdI methyltransferase resembles that of type I MTases, in contrast to the R.AhdI endonuclease which is typical of type II systems. AhdI appears to be a novel R-M system with properties intermediate between simple type II systems and more complex type I systems, and may represent an intermediate in the evolution of R-M systems.

Amino Acid Sequence↗