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2.
Cancer Nurs ; 13(6): 354-60, 1990 Dec.
Article in English | MEDLINE | ID: mdl-2276108

ABSTRACT

Pediatric oncology nursing has been identified as a stressful specialty, but the exact sources of the stress have not been comprehensively specified nor put into measurable form. Effective interventions can best be developed when the stressors are known and measured. The purpose of this study was to develop and test an instrument that could accurately and sensitively measure the job-related stressors for pediatric oncology nurses. A 61-item, visual analogue instrument, the Stressor Scale for Pediatric Oncology Nurses (SSPON), was inductively developed from interviews with 30 pediatric oncology nurses. Subsequently, the SSPON was tested in three geographically separated samples of pediatric oncology nurses (n = 78). After an item analysis, 11 items were deleted from the scale. Reliability of the SSPON was estimated using both stability and internal consistency methods. The test-retest correlation coefficient was 0.88, and the total scale alpha coefficient was 0.94. Content validity was estimated using a two-stage process of developmental and judgment quantification with a panel of three specialty nurses. Construct validity was estimated through testing of theoretically derived hypotheses and a cluster analysis. Findings indicated the SSPON is content valid. Six meaningful clusters that represented sources of job-related stress were identified and defined. The revised SSPON appears to have adequate psychometric properties for a new instrument.


Subject(s)
Nursing Staff, Hospital/psychology , Oncology Nursing , Pediatrics , Psychological Tests/standards , Stress, Psychological/diagnosis , Evaluation Studies as Topic , Humans , Reproducibility of Results , Stress, Psychological/epidemiology , Stress, Psychological/psychology
3.
Kidney Int ; 25(6): 880-5, 1984 Jun.
Article in English | MEDLINE | ID: mdl-6088886

ABSTRACT

Rat renal lymph contains 254 +/- 17 ng/ml (means +/- SEM, N = 20) of immunoreactive glandular kallikrein. Like the immunoreactive glandular kallikrein in plasma, it is biologically inactive. Gel filtration of renal lymph reveals profiles for immunoreactive glandular kallikrein, protein, and inhibition of trypsin and kallikrein which resemble those seen for plasma except that high molecular weight plasma components are reduced or missing in renal lymph. In contrast, gel filtration of thoracic lymph reveals immunoreactive glandular kallikrein and protein profiles which are indistinguishable from those seen with plasma. Renin levels are 170-fold higher in renal lymph than in thoracic lymph while angiotensin-converting enzyme levels are only 16% those of thoracic lymph. In keeping with the high renin and low converting enzyme activities, renal lymph contains high levels of angiotensin I. Immunoreactive glandular kallikrein levels in renal lymph, thoracic lymph and plasma do not show the striking differences observed for renin.


Subject(s)
Kallikreins/metabolism , Kidney/enzymology , Kinins/metabolism , Lymph/enzymology , Renin-Angiotensin System , Angiotensin I/metabolism , Angiotensin II/metabolism , Animals , Chromatography, Gel , Male , Molecular Weight , Peptidyl-Dipeptidase A/metabolism , Radioimmunoassay , Rats , Rats, Inbred Strains , Renin/metabolism
4.
J Biol Chem ; 256(20): 10634-9, 1981 Oct 25.
Article in English | MEDLINE | ID: mdl-7287727

ABSTRACT

Kininogen was isolated from human urine by batch adsorption with immobilized antibody to the immunologically identical heavy (H) chains of both high molecular weight (HMW) and low molecular weight (LMW) human plasma kininogens. All releasable kinin in the guanidinium chloride eluate was associated with kininogen antigen in gel filtration fractions. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the eluate gave major stained and antigenic bands corresponding to the major form of plasma LMW kininogen. Also, the staining patterns and antigenic profiles obtained upon alkaline disc gel electrophoresis of the urinary and plasma LMW kininogens were strikingly similar. When antibody to H chain was used in an indirect immunofluorescence technique, cytoplasmic staining was observed in cells of distal tubules and c cortical and medullary collecting ducts of human kidneys. No fluorescence was observed using antibody to the unique light (L) chain of plasma HMW kininogen and no intact HMW kininogen was found in urine by radioimmunoassay. We conclude that the kidney is a source of urinary kininogen, while the L chain antigen in urine probably represents filtered degradation products of plasma HMW kininogen.


Subject(s)
Kidney/analysis , Kininogens/analysis , Humans , Kidney/cytology , Kidney Cortex/analysis , Kidney Glomerulus/analysis , Kidney Tubules, Distal/analysis , Kininogens/urine , Kinins/urine , Macromolecular Substances , Microscopy, Fluorescence , Molecular Weight , Radioimmunoassay
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