Staff nutrition education with dietary intake of nursing home residents.
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Biomedical subjects
Publications and source records attributed to S Kim.
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Primary prevention of drug abuse is defined as a systematic effort through which curiosity-oriented drug experimenters are kept from becoming regular drug users. Following this definition, a model program entitled Ombudsman is evaluated. The hypothesis tested is: The proportion of students who no longer use drugs will be greater among those who have participated in the Ombudsman program than among those who have not. Some of the findings are: (1) the program is most effective with regard to "hard' drugs (greater than .001), but not with "social' drugs; (2) the program impact is most effective among younger students (p greater than .01).
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A questionnaire was developed, tested, and revised to produce an instrument ot measure the effect of a nutrition education program on the staff of a nursing home in future studies. The results of the questionnaire were recorded for future comparisons with similar groups. The results of this study showed that there were positive changes in nutrition information for staff members receiving the program as well as changes in their attitudes about assuming responsibility for food choices of residents. The Job Satisfaction Index for the 33 subjects filling out the pre-test questionnaire showed a below normal score for work, pay, and co-workers and a normal response for supervision and promotion. The number of subjects was too small for statements of significance, but the possibility for change shown in this study seems to indicate that the method should be used in a larger population study. The lesson evaluations indicated that the material was well presented and well received. The staff responded very positively to the videotape, Meals: Then and Now, and to the opportunity to use role-playing to practice using information received in the nutrition education program to improve and support adequate dietary intake by residents. In this project we explored the possibility of using a nutrition education program for the staff of a nursing home, non-professional as well as professional, in order to create an awareness and a change in attitude concerning their role in the nutritional care of the elderly resident. At the end of the last nutrition education lesson, 78 percent of the staff members felt able to talk to residents about their attitudes toward meals served at the nursing home and to encourage residents to make good food choices.
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Methylation of cytochrome c was studied in vivo using double label with L-[methyl-3H]methionine and DL-[2-14C]methionine. In pulse-chase experiments the cytochrome c associated with the mitochondrial fraction possessed a higher ratio of 3H/14C label, suggesting the presence of methylated cytochrome c. The appearance of methylated cytochrome c in mitochondria showed no lag phase. The inhibition of cytochrome c methylation in presence of cycloheximide indicated that both the methylation and protein synthesis were tightly coupled and cycloheximide selectively inhibited cytochrome c methylation. There was also an indication of selective turnover of incorporation methyl groups in preformed cytochrome c.
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A highly purified protein methylase III from Neurospora crassa or Saccharomyces cerevisiae specifically methylates a single lysine residue of position 72 of horse heart cytochrome c. The enzymatically methylated cytochrome c has been separated from the unmethylated counterpart species by isoelectric focusing. Simultaneously, the pI values of these two species were found to be 9.49 and 10.03, respectively. Since methyl substitution increases the basicity associated with the epsilon-amino group of lysine residues, the observed decrease in pI value is in opposition to the predicted increase. Space-filling models revealed the possibility of a hydrogen bond between the oxygen of amide of residue-70 asparagine and the epsilon-amino nitrogen of residue-72 lysine in unmethylated horse heart cytochrome C. the enzymatic methylation of residue-72 lysine tends to dissociate this hydrogen bond, thereby possibly inducing the shift of 'effective charge' of the protein molecule. This paper also deals with the pI values of cytochromes c from 13 different sources, determined by the isoelectric focusing technique.
In order to study the in vivo methylation of ghost membrane proteins, human erythrocytes were incubated with L-[methyl-3H]methionine. The [3H]methyl incorporation into the membrane components was observed in freshly prepared erythrocytes. Upon treatment of the methylated membrane at pH 7.4, 100 degrees C for 5 min, a condition which is known to hydrolyze protein-carboxyl methyl ester, 80% of the incorporated [3H]methyl was recovered as methanol. Cycloleucine, an inhibitor for S-adenosylmethionine synthetase, inhibited 70% of the methylation. The analyses of the methylated proteins by sodium dodecyl sulfate/polyacrylamide gel electrophoresis revealed two major methylated protein peaks which were tentatively identified as glycophorin A and band 4.5. This methylation pattern is similar to the in vitro methylation pattern when purified human ghosts were methylated with purified protein methylase II and S-adenosylmethionine (Galletti, P., Paik, W. K., and Kim, S. (1979) Eur. J. Biochem. 97, 221-227). It is concluded that carboxyl methylation of erythrocyte membrane proteins is the major methylation reaction in vivo in these membranes.
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Differential inhibitory effects of various chemicals on both formaldehyde formation and total macromolecular binding have been examined during oxidative demethylation of [14C]dimethylnitrosamine (DMN) by hamster liver microsomes. One group of chemicals such as diethyldithiocarbamate (DEDTC), aminoacetonitrile (AAN), 2-[(2,4-dichloro-6-phenyl) phenoxy]-ethylamine (DPEA), azide and ethanol inhibits both HCHO formation and total macromolecular binding. A second group of chemicals such as reduced glutathione, semicarbazide and N-(1-naphthyl)thiourea (NTU) inhibits macromolecular binding without appreciably affecting HCHO formation. Possible mechanisms of these differential inhibitory effects by these chemicals are discussed.
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