Breastfeeding and mothering one-handed.

This case study describes how a mother with a congenital below-elbow limb absence manages breastfeeding and child care. Information for the case study was gained from direct observation, detailed interviews, and the subject's written reflections. Literature review revealed that, worldwide, many women have upper limb deficiencies. Such deficits may occur congenitally from teratogens or other causes, or they may occur as a result of disease or trauma. In spite of recent technological advances, prostheses are restricted in their efficiency and are not frequently used. Support from others is a critical factor in enabling those with limb deficiencies to achieve an optimal quality of life, including during childbearing and childrearing. No published data to assist breastfeeding mothers with limb deficiencies was revealed. Specific practices are mentioned that promote self-confidence and capability with breastfeeding and fulfilling children's needs.

Demonstration of basic human-brain-specific proteins by the BASO-DALT system.

We used the BASODALT system (Cell 12: 1133--1142, 1977) of high-resolution two-dimensional gel electrophoresis to resolve proteins in extracts of human brain and, for comparison, those in nine other human organs. At least 180 protein-staining spots are visible on a BASODALT electrophoretogram of water-soluble human brain proteins. By electrophoresing extracts of different human organs, separately and mixed with brain extract, we could detect 14 basic spots that appear to be present in brain in concentrations at least 20-fold those in any other organ. Measurement of these new basic brain-predominant proteins may provide useful diagnostic information in neurological disorders.

A comparison of the evolutionary distribution of the two neuroendocrine markers, neurone-specific enolase and protein gene product 9.5.

One- and two-dimensional polyacrylamide gel electrophoresis followed by immunoblotting has been used to examine the phylogenetic distribution of the two neuronal and neuroendocrine proteins, neurone-specific enolase and protein gene product 9.5, in animal brains. A new immunoblotting procedure was used in which complex two-dimensional patterns of brain proteins were transferred to nitrocellulose paper simultaneously with the Coomassie Blue stain. This produced a copy of the blue spot pattern against which brown protein spots reacting in a specific antibody-immunoperoxidase procedure could be identified unequivocally. Extracts of human, bovine, sheep, rabbit, rat, guinea-pig, chicken, trout, and frog brains were examined. Proteins cross-reacting with antisera to the human forms of both proteins could be demonstrated in all species examined. This suggests that proteins corresponding to neurone-specific enolase and protein gene product 9.5 could have evolved at least 400 million years ago and have been highly conserved throughout evolution.