Biomedical subjects

F F Hall

Publications and source records attributed to F F Hall.

4 recordsLinked to original sources

PubMed1976

Lipoamide dehydrogenase in serum: a preliminary report.

Lipoamide dehydrogenase was identified in serum and the optimal conditions for its assay at 30 degrees C were defined. The pH optimum in tris(hydroxymethyl)aminomethane buffer is 7.8, and activity is inhibited if buffer concentration exceeds 100 mmol/liter. Saturating concentrations of the substrates NAD+ and lipoamide are 3 mmol/liter and 5 mmol/liter, respectively. Activity is decreased eightfold when lipoic acid is substituted for lipoamide. Activity is linearly related to enzyme concentration up to limiting absorbance change of 0.300 at 340 nm, and both within-day and day-to-day precision are satisfactory. Data suggest a normal range (2 SD) of 3-19 kU/liter. The highest value measured in serum was 473 kU/liter. A correlation with direct bilirubin concentrations (r equals 0.435, P less than 0.01) was found.

Bilirubin↗

PubMed1975

Immunoglobulin characterization of human pancreatic fluid.

Human pancreatic fluid obtained from 2 subjects, each with a traumatic pancreatic fistula, contained detectable levels of IgG, IgA, IgM, IdD, and IgE. Although the mean IgG/IgA ratio for 10 random specimens was 1.63, the relative concentration was estimated to be less than unity when extreme values were eliminated. The molecular weight of IgA in pancreatic fluid was found to be comparable to that of the IgA molecule in serum. The absence of secretory component in pancreatic IgA provides further evidence that pancreatic IgA and serum IgA are similar. Serial determinations of the immunoglobulins stored at 4 degrees C showed a progressive decrease of all immunoglobulins, the order of stability being IgG approximately equal to IgA larger than IgM approximately equal to IgD. The demonstrated proteolytic activity in the specimens could account for the immunoglobulin decay and for the variable detection of IgM and IgD in pancreatic-fluid specimens.

Abdominal Injuries↗

PubMed1975

Complement component analysis in angiodema. Diagnostic value.

Complement component analysis is valuable for differentiating the various types of angioedema. Patients with hereditary angioedema have decreased levels of C1 esterase inhibitor and C4 in the presence of normal amounts of C3 and C1q. Acquired C1 esterase inhibitor deficiency secondary to malignant disease is also manifested by depressed C1 esterase inhibitor and C4, but decreased C1q levels distinguish it from hereditary angioedema. Normal values for these complement components are found in persons with allergic angioedema.

Angioedema↗

PubMed1975

Improved high-resolution high-voltage paper electrophoresis system for use in screening for aminoacidopathies.

High-voltage paper electrophoresis of small samples of serum and urine at pH 6.0 resolves basic and acidic amino acids and separates them from the neutral amino acids. For separation and identification of the neutral amino acids, the appropriate area of the electrophoretogram is cut out, sewn onto a second sheet of paper, and rerun at pH 1.9. By this method, amino acids are rapidly resolved. It is suited for use with special procedures such as oxidation of biological fluid with performic acid and specific staining for confirmation of amino acid identification.

Amino Acid Metabolism, Inborn Errors↗