Factors associated with the practice of nursing staff sharing information about patients' nutritional status with their colleagues in hospitals.

BACKGROUND/OBJECTIVES: Nursing staff have an important role in patients' nutritional care. The aim of this study was to demonstrate how the practice of sharing a patient's nutritional status with colleagues was affected by the nursing staff's attitude, knowledge and their priority to provide nutritional care. SUBJECTS/METHODS: The participants were 492 nursing staff. We obtained participants' demographic data, the practice of sharing patients' nutritional information and information about participants' knowledge, attitude and priority of providing nutritional care by the questionnaire. We performed partial correlation analyses and linear regression analyses to describe the relationship between the total scores of the practice of sharing patients' nutritional information based on their knowledge, attitude and priority to provide nutritional care. RESULTS: Among the 492 participants, 396 nursing staff (80.5%) completed the questionnaire and were included in analyses. Mean±s.d. of total score of the 396 participants was 8.4±3.1. Nursing staff shared information when they had a high nutritional knowledge (r=0.36, P<0.01) and attitude (r=0.13, P<0.05); however, their correlation coefficients were low. In the linear regression analyses, job categories (ß=-0.28, P<0.01), knowledge (ß=0.33, P<0.01) and attitude (ß=0.10, P<0.05) were independently associated with the practice of sharing information. Nursing staff's priority to provide nutritional care practice was not significantly associated with the practice of sharing information. CONCLUSIONS: Knowledge and attitude were independently associated with the practice of sharing patients' nutrition information with colleagues, regardless of their priority to provide nutritional care. An effective approach should be taken to improve the practice of providing nutritional care practice.

Chemical modification of enzymes with activated magnetic modifier.

An activated magnetic modifier, which could render biological materials magnetic property, was synthesized in following two steps: oxidation of ferrous ions (Fe2+) with hydrogen peroxide in the presence of alpha, omega-dicarboxymethylpoly(oxyethylene) (DCPEG) to obtain DCPEG-magnetite (Fe3O4); free carboxyl groups in the DCPEG-magnetite were activated with N-hydroxysuccinimide. By coupling the activated magnetic modifier to amino groups of lipase or L-asparaginase, magnetic enzymes were prepared. They dispersed stably not only in aqueous solution but also in organic solvents with high enzymic activities. Magnetic enzymes were readily recovered from reaction mixture in a magnetic field of 6000 Oe without loss of enzymic activity.

Magnetic lipase active in organic solvents.

Magnetic lipase (magnetite particles coated with polyethylene glycol-modified lipase) was prepared in two steps: Lipase was coupled with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine, activated PEG2, to obtain polyethylene glycol-modified lipase, PEG-lipase. The PEG-lipase was added to the solution of ferrous (Fe2+)- and ferric(Fe3+)-ions with the pH value adjusted to 8.0-8.5 to obtain magnetic lipase. The magnetic lipase was dispersed in organic solvents such as benzene and 1,1,1-trichloroethane with the particle size of 120 +/- 60 nm. The colloidal solution was very stable and no aggregation occurred even after 5 days. A high enzymic activity (11.6 mumol/min/mg protein) for lauryl laurate synthesis was observed in 1,1,1-trichloroethane. The magnetic lipase was readily recovered from the organic solvents in a magnetic field of 6000 Oe without loss of the enzymic activity.

Ester synthesis at extraordinarily low temperature of -3 degrees C by modified lipase in benzene.

The lipoprotein lipase from Pseudomonas fluorescens was modified with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine. The modified lipase in which 55% of the amino groups in the enzyme molecule were coupled with polyethylene glycol was found to be soluble in benzene and catalyzed the reactions of ester synthesis, ester exchange, aminolysis and ester hydrolysis in benzene. The modified lipase had an extraordinary temperature-dependency: enzymic activity for methyl laurate synthesis from methyl alcohol and lauric acid increased with decreasing temperature and attained the maximum at the extremely low temperature of -3 degrees C. The optimum temperature for hydrolysis of methyl laurate was as low as -4 degrees C.

Activation and stabilization of asparaginase by anti-asparaginase IgG and its Fab.

Modified asparaginase, in which 4 tryptophan residues were modified with 2-hydroxy-5-nitrobenzyl bromide, had little enzymic activity and retained immunoreactivity [(1976) FEBS Lett. 65, 11-15]. Addition of IgG or its Fab towards asparaginase to the modified asparaginase gave rise to marked enhancement of the enzymic activity. Native asparaginase (4 subunits) lost the enzymic activity due to dissociation into subunits by dilution of the enzyme solution. However, in the presence of Fab, asparaginase did not lose enzymic activity on dilution, probably due to no dissociation into subunits occurring.

Modified lipoprotein lipase catalyzes ester synthesis in benzene. Substrate specificity.

Modified lipoprotein lipase catalyzed the synthesis of trilaurin from mono- or diacylglycerol and fatty acid and also the synthesis of ester from fatty acid and alcohol in benzene. In the ester synthesis reaction, the longer the chain length of fatty acid or alcohol, the higher the ester synthesis activity. The ester synthesis was competitively inhibited by fatty acids with branch of carbon chain at the position neighboring the carboxyl group. Other substrates including secondary and tertiary alcohols and carboxylic acids having benzene ring were tested and discussed in relation to the ester synthesis.

Fibrin suspension as a substrate fop plasmin: determination and kinetics.

Fibrin polymers formed from fibrinogen with thrombin in the presence of EDTA were suspended in a medium containing glucose, arabic gum and imidazole-HCl buffer and were sonicated at 20 kHz for 20 min to make a suspension containing fibrin particles of small size. The fibrin suspension was used as a substrate of plasmin for determining the enzymic activity of plasmin and plasminogen activated with urokinase. The kinetic study on the reaction of the fibrin particles with plasmin in the presence and the absence of fibrinogen revealed that Km value of fibrin for plasmin is 4.2 x 10(-7) M and the Ki value of fibrinogen is 1.2 x 10(-5) M.

Inhibition of E coli ATPase activity by a troponin component, TN-I, and by mitochondrial ATPase inhibitor.

The enzymic activity of Mg2+- or Ca2+-stimulated ATPase from Escherichia coli was inhibited by one of the troponin components, TN-I, and by mitochondrial ATPase inhibitor (F1-inhibitor). The inhibitory ability of component TN-I against Mg2+-stimulated AtPase activity was lost after digestion of component TN-I with trypsin. The Mg2+-stimulated ATPase activity inhibited by component TN-I was completely restored by the addition of another troponin component TN-C.

Faster determination of clottable fibrinogen in human plasma: an improved method and kinetic study.

Clottable fibrinogen in human plasma was determined by measuring spectrophotometrically the increase in turbidity with time due to the fibrinogen-fibrin conversion with thrombin. From the maximal absorbance, Amax, at 450 nm obtained 2 min or less after thrombin as added to plasma, we estimated the fibrinogen concentration in plasma of normal subjects and patients. Analysis of the rate of the absorbance increase yielded the Km value, 1.6 X 10(-5) mol/liter, which closely agrees with the Km of 1.2 X 10(-5) mol/liter obtained by analysis of the fibrinopeptides released from fibrinogen.