Scrubs, scrubs, who's got the scrubs?
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Biomedical subjects
Publications and source records attributed to K A Rosenthal.
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This paper describes an approach which can be used to increase both the speed and the sensitivity of a monoclonal antibody (MAb) based ELISA for human IIbIIIa by using a mixture of enzyme labeled MAbs (conjugates) and a one step incubation format (where analyte and conjugates were incubated simultaneously for 2 h in the MAb coated well). A simple competitive blocking method is described for mapping the relative epitopes of five monoclonal antibodies (MAbs) with minimum preparation of enzyme conjugate. This method permits the selection of three MAbs which recognize distinctly different epitopes, and are suitable for use in a one step ELISA format. Compared to the regular two step ELISA using two MAbs, this simple modification improves the assay sensitivity by three-fold and decreases the incubation time by 75%, while maintaining a high level of precision (2-15%). The assay is very specific and can accurately measure both recombinant and native IIbIIIa.
Infection of mononuclear cells by human immunodeficiency virus (HIV) begins with binding of the viral envelope glycoprotein, gp120, to its receptor, CD4. CD4 contains four extracellular immunoglobulin-like domains, the first of which (V1) is sufficient for HIV binding. V1 contains three sequences homologous to the antigen-complementarity-determining regions (CDR1 to -3) of immunoglobulin variable domains. While all three immunoglobulin CDRs are involved in antigen binding, only amino acids within and flanking the CDR2-like region of CD4 have been shown previously to be involved in gp120 binding. To investigate whether other regions in V1 take part in gp120 binding, we substituted alanine for each of 64 amino acids, including all of the hydrophilic residues in this domain. Mutations at four locations outside the CDR2-like sequence (amino acids 29, 59-64, 77-81, and 85) markedly affected gp120 binding, but not the overall structure of V1 as probed with eight conformationally sensitive monoclonal antibodies. Thus, the gp120-binding site of CD4 is not limited to the CDR2-like sequence and consists of several discontinuous segments. Several amino acids were identified that are critical for the conformation of V1; the importance of these residues suggests some differences in the folding of this domain compared to immunoglobulin variable domains. Three amino acid substitutions were found that increase the affinity for gp120 significantly (1.7- to 2-fold individually and 4.2-fold when combined), suggesting that it may be possible to improve the HIV-blocking ability of CD4-based molecules by increasing their gp120 binding affinity.
The information in this article is for a wide variety of nurses who find themselves in a teaching role: the critical care nurse orienting another nurse (experienced or new graduate); the critical care manager who needs to present an inservice program; and the educator or clinical specialist looking for a new way to present the same information. The author describes how self-paced modules for inservice education offer variety to learners since learners choose the teaching strategy that best suits their learning styles.
OBJECTIVE: To examine the relationship of patient-perceived and nurse-perceived caring behaviors. DESIGN: Descriptive. SETTING: Three not-for-profit hospitals in a large metropolitan western city. SUBJECTS: Thirty coronary care patients and 30 coronary care nurses. METHOD: Larson's nurse caring behaviors (CARE-Q) were rank ordered by the Q-sort method. RESULTS: The patient's study group perceived behaviors that involved technology as most important, which differed from nurses, who perceived listening as the most important caring behavior. CONCLUSIONS: This study supports the findings of other researchers that patients' and nurses' perceptions of important nurse caring behaviors are divergent.
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