PubMed Health⌕ Search

Biomedical subjects

K S You

Publications and source records attributed to K S You.

10 recordsLinked to original sources
PubMed1997

Learning from other lands. Caring for elderly demented Koreans.

The aims of the study reported here were to describe the socio-demographic characteristics of caregivers of demented elders in Korea and their care recipients and to compare the positive and negative meanings and outcomes of the caregiving experiences of caregivers who had admitted their elderly demented relative to a nursing home (G1: n = 24) and caregivers still caring for their elderly demented relatives at home (G2: n = 30). Most caregivers were female (80%), married (89%), and related to the care receiver as daughter-in-law (39%), daughter (22%), wife (15%), son (13%), or neighbor (6%). Social class differences were found between the home care and nursing home groups: the upper classes were significantly more likely to have placed their demented elder in a nursing home, whereas the low social classes were more likely to keep taking care of their demented elder at home instead of placing them in a nursing home. Caregivers who had admitted their relative to a nursing home (G1) reported significantly more difficulties from disturbed sleep, disrupted children's studies, and limited personal life when they were caring for the elder at home (p < .05). Caregivers in the home care group (G2) had significantly greater satisfaction in serving as a model for their children and practicing religion (p < .05), and they also reported a better relationship with the care receiver than those who have placed their demented elder in a nursing home, although the difference in this case was not significant.

Adult↗
PubMed1996

[Effect of hemin in treating hemorrhagic anemia and toxicity].

AIM: To study the effect of hemin in treating hemorrhagic anemia and toxicity. METHODS: Fifty rats with hemorrhagic anemia were randomly divided into 5 groups with different dosage of hemin (93, 168, 300 mg.kg-1.d-1), ferrous gluconate (FG 300 mg.kg-1.d-1), and water, ig for 7 d. Twenty mice fed with hemin (6.0 g.kg-1.d-1) in 24 h for observing acute toxicity effects. Long-term toxicity were observed in 80 rats given hemin (0.65, 1.3, 2.6 g.kg-1.d-1) in 3 months. RESULTS: Hb of the rats of corresponding groups were 66-->121, 71-->141, 66-->148, 69-->140, and 67-->112 g.L-1. There were no adverse effects observed on acute toxicity test. No abnormalitis were found in hemogram, liver renal function test, and autopsy. CONCLUSION: Hemin had a better effect than FG and no adverse effect was found in hemin.

Anemia, Iron-Deficiency↗
PubMed1985

Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions.

The pyridine nucleotide (NAD and NADP)-linked enzymes are a large class of enzymes constituting approximately 17% of all classified enzymes. When these enzymes catalyze their reactions, the hydride transfer between the substrate and the reaction site (i.e., C-4 of the nicotinamide/dihydronicotinamide ring) of the coenzyme takes place in a stereospecific manner. Thus, in the reaction of oxidation of the reduced coenzyme, one group of enzymes catalyzes the extraction of only the hydrogen having the R configuration at the No. 4 carbon, while the other group catalyzes the removal of only that with the S configuration. Because this aspect of enzyme stereospecificity provides essential information for a given enzyme's reaction mechanism, active site structure, and evolutionary relationship with other enzymes, intensive effort has been made to establish the stereospecificities of as many enzymes as possible. This review presents the compilation of the stereospecificities of these enzymes. Some empirical rules, which are useful but not definitive, in predicting a given enzyme's stereospecificity are also described. In addition, the stereospecificity in enzymatic reactions is compared to the stereo-preference in chemical oxidoreduction of the coenzyme. In order to elucidate the mechanism for the enzyme stereospecificity, the conformations of the coenzyme in free-state and enzyme-bound state are extensively discussed here.

Adenosine Monophosphate↗
PubMed1976

Purification and properties of a low molecular weight protein factor of mitochondrial energy-linked functions.

1. A soluble protein with a molecular weight of 11-12-10(3) has been isolated from bovine-heart mitochondria, which stimulates the following ATP-dependent reactions of submitochondrial particles treated with 0.6 mM EDTA and 1 M NH4OH: reverse electron transfer from succinate to NAD, transhydrogenation from NADH to NADP, and ATP-Pi exchange. The factor has no effect on the NADH oxidase, succinate oxidase and ATPase activities of the particles. 2. The stimulatory effect of the factor in the ATP-dependent reduction of NAD by succinate is 12 mumol-min-1-mg-1 of the factor protein. However, the NH4OH-EDTA treated particles are saturated for maximal activation of the above reaction by very small amounts of the factor (about 20-40 mug factor per mg particle). 3. Electrophoresis of the factor preparation on polyacrylamide gels showed a single protein band plus a nonprotein material which moved at the dye front and was weakly stained with Coomassie Blue. The protein was shown to be required for activation of the particles; whether the fast-moving, nonprotein material is also required is not known. 4. The factor is inhibited by mercurials and N-ethylmaleimide. The former, but not the latter, inhibition is completely reversed by 1,4-dithiothreitol. 5. The NH4OH-EDTA treated particles are also stimulated by rutamycin up to about 0.1 nmol of rutamycin per mg particle; higher rutamycin concentrations inhibit. Depending on the particle preparation, the factor stimulates up to about 3 nmol per mg particle, but does not inhibit at higher concentrations. In addition, under certain conditions in which appropriate concentrations of rutamycin fail to stimulate the particles, the factor still does.

4-Chloromercuribenzenesulfonate↗
PubMed1975

Purification and properties of malate dehydrogenase from Pseudomonas testosteroni.

Nicotinamide adenine dinucleotide-linked malate dehydrogenase has been purified from Pseudomonas testosteroni (ATCC 11996). The purification represents over 450-fold increase in specific activity. The amino acid composition of the enzyme was determined and found to be quite different from the composition of the malate dehydrogenases from animal sources as well as from Escherichia coli. Despite this difference, however, the data show that the enzymatic properties of the purified enzyme are remarkably similar to those of other malate dehydrogenases that have been previously studied. The Pseudomonas enzyme has a molecular weight of 74,000 and consists of two subunits of identical size. In addition to L-malate, the enzyme slowly oxidizes other four-carbon dicarboylates having an alpha-hydroxyl group of S configuration such as meso- and (-) tartrate. Rate-determining steps, which differ from that of the reaction involving L-malate, are discussed for the reaction involving these alternative substrates. Oxidation of hydroxymalonate, a process previously undetected with other malate dehydrogenases, is demonstrated fluorometrically. Hydroxymalonate and D-malate strongly enhance the fluorescence of the reduced nicotinamide adenine dinucleotide bound to the enzyme. The enzyme is A-stereospecific with respect to the coenzyme. Malate dehydrogenase is present in a single form in the Pseudomonas. The susceptibility of the enzyme to activation or inhibition by its substrates-particularly the favoring of the oxidation of malate at elevated concentrations-strongly resembles the properties of the mitochondrial enzymes. The present study reveals that whereas profound variations in chemical composition have occurred between the prokaryotic and eukaryotic enzymes, the physical and catalytic properties of malate dehydrogenase, unlike lactate dehydrogenase, are well conserved during the evolutionary process.

Amino Acids↗