Biomedical subjects
G Skinner
Publications and source records attributed to G Skinner.
Provider-patient communication and metabolic control.
OBJECTIVE: To determine whether nurses' and NIDDM patients' communication styles during consultations are related to subsequent metabolic control and to examine factors influencing patterns of communication in these consultations. RESEARCH DESIGN AND METHODS: A total of 47 NIDDM patients participated in the study and completed the following procedures: 1) assessment of baseline HbA1, 2) attended 3.5 days of diabetes education, 3) returned in 1 mo for a follow-up consultation with a nurse, and (4) returned in 9-12 wk for a follow-up HbA1 assessment. The communication variables coded from the consultations were the frequency with which nurses produced controlling, informative, and patient-centered utterances and the frequency with which patients sought information, engaged in decision making, and expressed negative affect. RESULTS: The results were as follows: 1) patients experienced poorer metabolic control after interacting with nurses who were more controlling and directive in their communication with patients (r = 0.39, P < 0.01); 2) the nurses' use of patient-centered responses was directly related to the degree to which patients expressed feelings (r = 0.34, P < 0.01) and exhibited decision-making behavior (r = 0.62, P < 0.01); and 3) several of the nurses' and patients' communicative behaviors were related to patient characteristics such as age, sex, education, and baseline HbA1 levels. CONCLUSIONS: The results suggest that providers' attempts to exert considerable control during consultations with NIDDM patients may be counterproductive and contribute to poorer outcomes. The findings also indicate that patient-centered behaviors (e.g., encouraging the patient's involvement, respecting the patient's opinion, and offering support) facilitate the patient's ability to be an active participant in the consultation.
A kinetic study of the photochemical inactivation of adenylate kinases of Mycobacterium marinum and bovine heart mitochondria.
Using incident light energy of about 76 mW.cm-2 in a dye-sensitized photooxidation reaction, we have investigated the possible involvement of one or both of the histidine residues in the catalytic activity of adenylate kinase (ATP:AMP phosphotransferase) of Mycobacterium marinum. We have done this by investigating the kinetics of photochemical inactivation of the enzyme. At pH 7.4, the kinetics of photoinactivation are biphasic with two different pseudo-first-order rate constants. Adenosine 5'-pentaphospho 5'-adenosine (Ap5A), ATP and, to some extent, AMP, all gave protection to the enzyme from inactivation. Amino-acid analysis of the photoinactivated enzyme indicated the loss of the two histidine residues. This, and the fact that photoinactivation occurred faster at alkaline compared to acidic pH, indicated the involvement of the histidine residues in the catalytic activity. A mathematical model is developed which assumes that both histidine residues are required for maximal catalytic activity: one is located peripherally, is exposed, and therefore is readily photooxidized (pseudo-first-order rate constant, k1 = 1.3.10(-2)s-1), while the other is located at the active site, involved in substrate-binding and is shielded (pseudo-first-order rate constant, k2 = 2.9.10(-4)s-1). However, this shielded histidine could be exposed and made more accessible to photooxidation either by raising the pH above 10, or alternatively, by the addition of 8 M acetamide (or 6 M guanidine). Under these conditions, which apparently cause unfolding of the protein molecule, the kinetics of photoinactivation change from biphasic to monophasic, suggesting that both histidine residues are equally exposed and are photooxidized at the same rate. Unlike the enzyme from M. marinum, adenylate kinase from bovine heart mitochondria shows monophasic kinetics of photoinactivation at pH 7.4, suggesting that only one of the six histidine residues is essential for catalytic activity, or if more than one, then they all must be equally exposed. Further, ATP, AMP or Ap5A did not provide protection against photoinactivation, suggesting that the histidine residue(s) involved in the catalytic activity must remain exposed after the substrates bind at the active site of the mitochondrial enzyme.
Herpes simplex: a cure for some ills.
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Chemosterilization of the cabbage root fly under field conditions.
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What do practicing nurses want to know?
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Quantitative determination of haptoglobin (HAP) in human and bovine sera by capillary zone electrophoresis (CZE).
This study describes an original assay for serum haptoglobin determination by measuring the capacity of human haptoglobin (hHAP) and bovine haptoglobin (bHAP) to bind haemoglobin (Hb) as established by capillary zone electrophoresis (CZE). This method involves the addition of Hb in excess to the serum and the separation of the HAP-Hb complexes from free haemoglobin by CZE. Protein migration was recorded at a wavelength of 415 nm which reveals Hb alone (free or bound), and the concentration of HAP was indirectly estimated by measuring bound Hb. Different CZE conditions and the peak migration time of Hb from various species (human, equine, bovine, canine) were investigated. The electrophoretic separation of free human Hb (hHb) in excess and the hHAP-hHb complex was fully achieved by CZE, allowing a quantitative determination of hHAP. However, bovine haemoglobin (bHb) bound to bHAP and free bHb were poorly separated under the same conditions. The best detachment between bHAP-Hb complexes and free Hb was only attained in the bovine sample by use of canine haemoglobin (cHb). CZE assays performed with cHb gave very close values to those of a classic photometric method which measured the peroxidase activity of the haptoglobin-cyanmethaemoglobin complexes (y = 1.0168x - 0.072; r2 = 0.97). CZE assay was fast (< 10 min), inexpensive, did not require the use of a specific antibody and was reproducible (coefficient of variation, CV 3.6%).
The history of surgical instruments.
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