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L M Killingsworth

Publications and source records attributed to L M Killingsworth.

At least 19 recordsLinked to original sources
PubMed1995

Electrophoresis-tutor: an image-based personal computer program that teaches clinical interpretation of protein electrophoresis patterns of serum, urine, and cerebrospinal fluid.

High-resolution protein electrophoresis of serum, urine, and cerebrospinal fluid (CSF) can aid in the diagnosis of multiple myeloma, amyloidosis, macroglobulinemia, multiple sclerosis, and other diseases. Electrophoresis-Tutor is a personal computer program based on approximately 150 digital images that teaches the clinical interpretation of agarose gel electrophoretic patterns. The program is divided into the following sections: introduction, CSF, serum, urine, review of disease states, program navigator, and final exam. The CSF section describes normal and abnormal CSF findings with emphasis on oligoclonal banding, as seen in the CSF of patients with multiple sclerosis. The serum section emphasizes monoclonal gammopathy patterns but also has detailed descriptions of inflammation, liver disease, protein-losing disorders, genetic deficiencies, and other patterns. Monoclonal gammopathy is described in the context of specific associated clinical conditions (e.g., myeloma, amyloidosis). For each monoclonal gammopathy example, results of standard electrophoresis, densitometry, and immunofixation are presented. The review of disease states uses animation to illustrate the development and remission of a variety of pathological patterns. The program navigator allows the user to jump quickly to any place in the program. The optional exam contains 20 questions, and detailed feedback is given after each question. Electrophoresis-Tutor can be used as a stand-alone teaching tool, a companion to traditional instruction, or a reference source.

Blood Proteins↗
PubMed1982

Clinical applications of protein determinations in biological fluids other than blood.

Over the past decade, significant improvements in immunochemical and electrophoretic techniques have enabled collection of heretofore unavailable data on proteins in biological fluids, greatly increasing our understanding of protein physiology in the various body compartments and providing the foundation for clinical use of protein analysis in body fluids. The most striking advance has been in the diagnosis of demyelinating disease through the use of serum/cerebrospinal fluid protein ratios and the morphological evaluation of immunoglobulin banding patterns. These laboratory tests are now considered obligatory for any patient in whom demyelinating disease is suspected as the cause of neurological dysfunction. Cerebrospinal fluid protein data can also be helpful in quantitating the permeability of the blood/cerebrospinal fluid barrier in many inflammatory or infectious central nervous system disorders. Assays of individual proteins in urine can help distinguish between different types of proteinuria, and can give quantitative data on the selectivity of the glomerulus and the reabsorbing capacity of the tubules. The protein content of saliva, synovial fluid, and milk has also been well characterized, and is clinically applicable to a wide range of disorders.

Animals↗
PubMed1979

Plasma protein patterns in health and disease.

The complex nature of protein metabolism has made interpretation of serum protein data a difficult task. Interpretive efforts can be facilitated by use of protein profiles which consist of quantitative immunochemical data combined with qualitative electrophoretic patterns. These profiles can be designed to clarify physiological relationships and emphasize pathological conditions through pattern recognition. This review will present protein profiles observed in acute, subacute, and chronic inflammation: liver diseases, protein losing disorders, plasma cell dyscrasias, humoral immune deficiencies, autoimmune diseases, genetic deficiency states, and other disorders. The value of consultative interaction and the use of combined profiles in the assessment of a patient's protein status will be covered. A discussion of protein patterns in normal individuals will include data on day-to-day, age- and sex-related variation. A section on management of protein data will present various approaches to profile reporting. Graphical report formats which minimize the time required for information transfer and simplify assimilation of results will be emphasized.

Adolescent↗
PubMed1976

Factors contributing to intra-individual variation of serum constituents: Physiological day-to-day variation in concentrations of 10 specific proteins in sera of healthy subjects.

Using an automated immunoprecipitin method, we assayed human sera for 10 proteins: haptoglobin, orosomucoid, transferrin, alpha1 antitrypsin, alpha2-macroglobulin, IgG, IGa, IgM, complement C3, and complement C4. Blood from 14 healthy subjects (25-40y) was sampled on six separate days. From each venipuncture serum was divided into four eliquots; two were assayed on the day of venipuncture and two were frozen and kept until the end of the study, when all of the frozen samples were analyzed in one batch. With this experimental design, batch-to-batch analytical variation could be estimated, and we avoided confounding it with the biological variation. Data analysis was based on the analysis of variance technique. The average physiological intra-individual coefficient of variation ranged from 2.5% for transferrin to 11.1% for orosomucoid. THe interindividual variation ranged from 9.5% for transferrin to 70.5% for haptoglobin and the ratio between intra-individual variation and interindividual variation ranged from 0.66 for IgM to 0.26 for orosomucoid and transferrin.

Adult↗
PubMed1975

Automated immunochemical method for determination of urinary protein of plasma origin.

An automated continuous-flow procedure has been developed for the rapid determination of urinary proteins of plasma origin. Antiserum to whole human plasma was used as the reagent, and the antigen-antibody reactions were quantitated by nephelometry. By adding polyethylene glycol (mol wt 6000-7500) to the reaction medium, reaction time was decreased to less than 3 min; no sample blanks were required; and samples were analyzed at a rate of 70 per hour. Recovery studies yielded an average of 98.5% of the added protein. In-run replicate precision (CV) of the method was 1.45%; day-to-day precision was 2.58%.

Autoanalysis↗