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1.
J Healthc Inf Manag ; 15(3): 307-18, 2001.
Article in English | MEDLINE | ID: mdl-11642147

ABSTRACT

It has become abundantly clear that standards of recording clinical terms in human-readable, computer-processable format are indispensable. Controlled medical terminology is the missing link in health information standards (in fact, medical terminology can be viewed as the mother of all standards); its absence interferes with the business of healthcare and impedes the core processes of healing and maintaining health. Medicine has lacked the controlled common medical vocabulary that would enable universal sharing of data at the point of care and ensure reliable information for determining health intervention effectiveness. Simple clinical and code content alone has proven insufficient for healthcare enterprises to successfully manage the terminology problem; the "lexical runtime engine," formerly called a vocabulary server (VOSER), which manages the vocabulary ontology and serves up the relevant vocabulary to users of applications in the clinical environment, has recently become a reality.


Subject(s)
Database Management Systems , Medical Informatics Applications , Medical Records Systems, Computerized , Terminology as Topic , Vocabulary, Controlled , Humans , Information Storage and Retrieval , Quality Assurance, Health Care , Software Design
2.
J Healthc Inf Manag ; 15(3): 319-30, 2001.
Article in English | MEDLINE | ID: mdl-11642148

ABSTRACT

A number of clinical coding and vocabulary schemes are in use in healthcare enterprises today. Most of them are weak in light of the qualities that characterize adequate controlled medical terminologies, as outlined in Part One of this review. Here we look at the major code and terminology sets with a critical eye, as well as suggest practical steps to enable health industry information system purchasers and users to move forward with their effort to use common terminology to improve the quality, service, and knowledge in their enterprise.


Subject(s)
Medical Informatics Applications , Medical Records Systems, Computerized/classification , Terminology as Topic , Vocabulary, Controlled , Abstracting and Indexing , Forms and Records Control , Humans , Quality Assurance, Health Care , United States
4.
J Obstet Gynecol Neonatal Nurs ; 29(5): 459-64, 2000.
Article in English | MEDLINE | ID: mdl-11012124

ABSTRACT

Motherhood as biologic destiny for women, has been long assumed. As nurses who aid women struggling with the demands of career and motherhood, we need to question this assumption. An exploration of feminist theory offers nurses ideas (and perhaps permission) to question the purpose and effects of mothering and the effects of mothering on women in our culture. Additionally, parallels between motherhood and the nursing profession are drawn.


Subject(s)
Feminism/history , Mothers/history , Cultural Characteristics , Female , History, 20th Century , Humans , Nursing , Political Systems/history , United States , Women's Rights/history
5.
Infect Immun ; 58(10): 3272-8, 1990 Oct.
Article in English | MEDLINE | ID: mdl-2401565

ABSTRACT

An approximately 15,000-dalton outer membrane lipoprotein of Haemophilus influenzae, the Hi-PAL (P6) protein, has been shown to elicit bactericidal and protective antibodies against both type b and nontypeable H. influenzae strains and is a vaccine candidate for these organisms. To determine whether the lipid modification of this protein is required for immunogenicity or the elicitation of biologically active antibodies, a genetic fusion was constructed that contains the sequence of mature Hi-PAL fused to the polylinker region of pUC19. The protein expressed by this clone does not contain detectable lipid and was purified to homogeneity. This recombinant fusion protein, rPAL, elicited a strong immune response when injected into rabbits, and the antiserum reacted well with native Hi-PAL. The antiserum was bactericidal against a number of clinical nontypeable strains, duplicating the activity of anti-Hi-PAL. The anti-rPAL antiserum was also protective against type b bacteremia in the infant rat model. These results demonstrate that purified rPAL elicits antibodies with biological activities that are similar to those of anti-Hi-PAL antibodies. Thus, the lipid component of Hi-PAL is not required for either immunogenicity or elicitation of biologically active antibodies.


Subject(s)
Bacterial Outer Membrane Proteins/immunology , Fatty Acids/immunology , Haemophilus influenzae/immunology , Acylation , Amino Acid Sequence , Animals , Antibodies, Bacterial/biosynthesis , Antibodies, Monoclonal , Bacterial Outer Membrane Proteins/genetics , Blotting, Western , Electrophoresis, Polyacrylamide Gel , Haemophilus influenzae/genetics , Immunization , Molecular Sequence Data , Palmitic Acid , Palmitic Acids , Protein Sorting Signals/genetics , Rabbits , Rats , Recombinant Fusion Proteins/immunology
6.
J Biol Chem ; 263(20): 9790-4, 1988 Jul 15.
Article in English | MEDLINE | ID: mdl-3290214

ABSTRACT

We have purified to homogeneity a peptidoglycan-associated protein from Haemophilus influenzae. Our purification process used differential extraction of cell envelopes with nondenaturing detergents. Solubilization of this protein was accomplished by heating a peptidoglycan-enriched subcellular fraction in the presence of one of several nondenaturing detergents at 55-60 degrees C. The purified protein migrated as a single band, with a Mr approximately 15,000, following sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This protein contains covalently linked fatty acids, is rich in tyrosine, but lacks methionine and tryptophan. Amino acid analysis also revealed the presence of glycerylcysteine, which has been shown to be the site of fatty acylation in other bacterial lipoproteins. Over 87% of the primary structure has been determined by sequencing high pressure liquid chromatography purified fragments derived from several endoproteinase digests. This protein belongs to a family of proteins, known as peptidoglycan associated lipoproteins, which appear to be components of the outer membranes of most Gram-negative bacteria.


Subject(s)
Bacterial Outer Membrane Proteins , Haemophilus influenzae/analysis , Lipoproteins/isolation & purification , Peptidoglycan/isolation & purification , Proteoglycans , Amino Acid Sequence , Amino Acids/analysis , Chromatography, High Pressure Liquid , Detergents , Electrophoresis, Polyacrylamide Gel , Endopeptidases/metabolism , Escherichia coli/analysis , Escherichia coli Proteins , Fatty Acids/analysis , Hot Temperature , Molecular Sequence Data , Molecular Weight , Sequence Homology, Nucleic Acid , Solubility
7.
Biochim Biophys Acta ; 497(1): 323-8, 1977 Mar 29.
Article in English | MEDLINE | ID: mdl-321036

ABSTRACT

The mode of biosynthesis of the thiazole moiety of thiamine, 4-methyl-5beta-hydroxyethyl thiazole (MHET) was studied using Salmonella typhimurium as test organism. It was shown by isotope incorporation experiments, that the sulfur atom, but not carbon-3, of cysteine is incorporated into MHET, indicating a separation of the sulfur atom of cysteine from the carbon chain during incorporation. Isotope competition experiments revealed that the incorporation of [35S]cysteine is not significantly diluted by the presence of methionine, homocysteine, and glutathione. No incorporation of label from [14C]glutamate and [14C]formate was observed, leaving the origin of the five-carbon unit still in doubt.


Subject(s)
Salmonella typhimurium/metabolism , Sulfur/metabolism , Thiamine/biosynthesis , Cysteine/metabolism , Models, Chemical
8.
Biochim Biophys Acta ; 437(1): 229-37, 1976 Jun 23.
Article in English | MEDLINE | ID: mdl-779848

ABSTRACT

The mechanism of biosynthesis of 4-methyl-5-beta-hydroxyethyl thiazole, the thiazole moiety of thiamine was studied in Salmonella typhimurium. Using the adenosine derepression technique the incorporation of various 14C-labeled precursors was determined. We found that;e1Me-14C]methionine, [2-14C]methionine, [U-14C]alanine, and [2-14C]glycine were not incorporated whereas [2-14C]tyrosine was incorporated. Degradation of the 4-methyl-5-beta-hydroxyethyl thiazole obtained after [2-14C]tyrosine incorporation revealed that all of the activity was located on carbon-2. These findings are discussed and compared with previous findings concerning 4-methyl-5-beta-hydroxyethyl thiazole biosynthesis.


Subject(s)
Salmonella typhimurium/metabolism , Thiamine/biosynthesis , Thiazoles/metabolism , Alanine/metabolism , Glycine/metabolism , Methionine/metabolism , Tyrosine/metabolism
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