Follow-up study of owner attitudes toward home care of paraplegic dogs.

A questionnaire was mailed to 30 owners of paraplegic dogs who had been caring for their dogs at home for 3 to 72 months. It was designed to collect information on demographic variables, duration of ownership and paralysis, age of the pet, pet/owner relationship, owner expectations and perceptions of the pet's quality of life, problems the pet experienced, effect that maintaining a paralyzed pet had on the owners' quality of life, and whether use of a cart was beneficial. Significant correlation was found between prior expectations that the pet would lead a high-quality life and perception that the pet, in fact, had a high quality of life during paralysis (r2 = 0.61, P = 0.01). Owners who had anticipated that extra work would be necessary to care for their paraplegic dog had a more positive attitude toward home care (r2 = 0.55, P = 0.03). Overall, owners involved in the study were satisfied with all aspects of maintaining paraplegic dogs at home. Our findings support the feasibility of dedicated owners successfully maintaining small (average body weight, 9 kg) paraplegic dogs at home for extended periods.

Hemin binding to serum proteins and the catalysis of interprotein transfer.

The reaction of hemin (Hm) with human hemopexin (Hx) has been studied in a mixed dimethyl sulfoxide (Me2SO)-water solvent system and in aqueous caffeine solutions. In both media, the kinetics could be described by a single, second-order process: (formula - see text) with k = 1.8 X 10(6) M-1 s-1 in 40% Me2SO-water [pH 7.4, mu = 0.2 M (NaCl)] and k = 3.9 X 10(7) M-1 s-1 in water [pH 7.4 mu = 0.2 M (NaCl), [caffeine] = 0.025 M]. The reaction shows an ionic strength dependence consistent with a residual 1+ to 2+ charge in the vicinity of the binding region of the protein. The kinetics of the transfer of hemin from albumin to hemopexin (formula - see text) were studied as a function of concentration, ionic strength, pH, and temperature. In experiments conducted at 3 less than or equal to [Alb]0/[Hx]0 less than or equal to 20 where the transfer kinetics are first order, k' = 5 X 10(-3) S-1 at mu = 0.3 M (NaCl), pH 7.1; the reaction is strongly dependent on ionic strength and choice of electrolyte. The addition of imidazole catalyzes this transfer process via a ligand-mediated pathway with k' = 5 X 10(-3) + 21[Im]T2. At [Alb]0/[Hx]0 = 92, the noncatalyzed transfer reaction is second order. From the kinetic analysis of the reaction under these conditions, an estimate is made of the distribution of hemin between the two proteins at concentration levels which are characteristic of serum. The association of hemin and hemopexin is approximately 30 times faster than that of hemin and albumin, a finding consistent with the recycling function of hemopexin during heme transport to the liver parenchymal cells.