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Biomedical subjects

J T Grace

Publications and source records attributed to J T Grace.

At least 19 recordsLinked to original sources
PubMed1995

Families and nurses: building partnerships for growth and health.

The newborn's social and emotional development depends on a relationship in which attention, affect, and information are shared with the mother. Young, disadvantaged families may encounter characteristic difficulties in maintaining these social relationships. Partnerships for health between nurses and disadvantaged clients require sharing similar relationships, and they present parallel challenges.

Child Development↗
PubMed1993

Mothers' self-reports of parenthood across the first 6 months postpartum.

A postpartum measure, What Being the Parent of a New Baby is Like, was administered to explore the development of maternal role for mothers (N = 76) at 1, 3, 4 1/2, and 6 months postpartum. Individual differences were relatively stable across time and accounted for much more variance than time effects. Mean scores on the Centrality (of baby) and Help (with parenting tasks) subscales decreased over time, and Evaluation (satisfaction with role performance) and Lifechange subscale scores increased. Primiparas demonstrated the steepest mean increase in Evaluation scores over time. Mean Evaluation scores for first- (n = 29) and second-time mothers (n = 33) were similar, but mothers of three or more children (n = 14) had significantly higher scores. Parity was also related inversely to amount of life change, and maternal education was related inversely to Evaluation and Centrality scores. Demographic, subscale, and contextual variable interrelationships were generally consistent with maternal role adaptation theory. Findings also suggest that parity effects are more complex than a dichotomous primipara/multipara representation.

Adaptation, Psychological↗
PubMed1975

Pharmacokinetics of guanazole in patients with acute myelocytic leukemia.

Levels of guanazole (GZ) in plasma and packed cells were determined after a single tracer dose of 14C-guanazole or during a 5-day continuous intravenous therapeutic infusion of unlabeled drug to 5 patients with acute myelocytic leukemia (AML). The levels of unlabeled drug were determined colorimetrically. GZ infected as a tracer dose was rapidly distributed in an apparent volume of 0.61 l/kg, which is somewhat less than that of total body water, and the drug appeared to be eliminated essentially unchanged by glomerular filtration. The mean apparent volume of distribution increased by about 15% during infusion. An increase of 60% was also noted in the half-life (t1/2) values, with a concimitant decrease in the mean value of renal clearance rate by 40%, except in 1 case. The study demonstrates that monitoring levels of guanazole is possible during infusion therapy and indicates that the data could be used to evaluate pharmacokinetic parameters predicting the time-course of such levels in patients.

Adult↗
PubMed1970

Protection of vaccinia from heat inactivation by nucleotide triphosphates.

The presence of adenosine triphosphate, guanosine triphosphate, cytosine triphosphate, or uridine triphosphate reduced the rate of inactivation of vaccinia when heated at 50 C. The virus-associated nucleoside triphosphate phosphohydrolases (adenosine triphosphatase, guanosine triphosphatase, cytosine triphosphatase, and uridine triphosphatase) and ribonucleic acid polymerase were also protected from heat inactivation by these compounds. These obervations are best explained by postulating that ribonucleoside triphosphates bind to enzymes in the virus particle, and that these enzyme-substrate complexes are more resistant to thermal denaturation than are the enzymes without their substrates. The kinetics of heat inactivation of the vaccinia ATP phosphohydrolase activity is biphasic, suggesting that there are two proteins in the vaccinia particle that have this enzyme activity but they have different kinetics of heat inactivation. Any of the vaccinia-associated nucleotide phosphohydrolase activities are protected from heat inactivation by the presence of any one of the respective nucleoside triphosphates. This observation suggests that there is a single enzymatic site in vaccinia that is able to react with any ribonucleoside triphosphate.

Adenosine Triphosphatases↗