Family function, respiratory illness, and otitis media in urban black infants.

Associations between maternal perceptions of family functioning and rates of infant presentation for respiratory illness and otitis media were analyzed using data collected prospectively in a sample of 114 urban black mother-infant pairs. Family functioning was evaluated using the Family APGAR, truncated versions of Olson's FACES II cohesion and adaptability subscales, and a shortened version of Hudson's Index of Family Relationships. Lower maternal scores of family function were significantly associated with higher rates of physician visits for infant respiratory illness and otitis media during the first 15 months of life. This correlation persisted when controlled for breast feeding. Maternal perceptions of family function, including those tested antenatally, may be useful in identifying infants in similar populations who are at risk for increased frequency of visits to the family physician for respiratory illness and otitis media.

Location of heme a on subunits I and II and copper on subunit II of cytochrome c oxidase.

A systemic study has been made of copper and heme a binding to subunits of beef heart cytochrome c oxidase. Copper and heme a were readily mobilized by ionic detergents, high ionic strengths, temperatures above 0 degrees C, thiol compounds, and gel-bound peroxides and free radicals when the subunits of the oxidase were dissociated from one another during polyacrylamide gel electrophoresis. Most subunits showed some affinity for heme a and copper under these conditions. However, in the presence of specific mixtures of ionic and nonionic detergents (e.g. 0.1% sodium dodecyl sulfate, 0.025% Triton X-100) at temperatures below 0 degrees C and in buffers of low ionic strength using 10 to 12% polyacrylamide gels preelectrophoresed for 3 days with thioglycolate, about 90% of the Cu was found on subunit II (Mr = 24,100), and heme a was found in equal amounts of subunits I (Mr = 35,800) and II. The oxidized-reduced and reduced-CO absorption spectra of these subunits resembled those of cytochrome c oxidase. It appears probable that in the native enzyme, subunit I contains heme a and subunit II contains copper and heme a. A relationship of mammalian cytochrome c oxidase to the two-subunit microbial cytochrome oxidase systems appears to exist.