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Biomedical subjects

F E Kaiser

Publications and source records attributed to F E Kaiser.

79 records · Page 5Linked to original sources
PubMedDate not supplied

Tablet-breaking ability of older persons with type 2 diabetes mellitus.

PURPOSE: The purpose of this study was to assess the ability of older persons with type 2 diabetes to accurately break in half 2 different formulations of micronized glyburide tablets. METHODS: Thirty persons with type 2 diabetes, over age 70, were recruited from the St Louis University geriatric clinics. Participants were randomly assigned to 2 groups. Group A broke 30 Glynase Prestabs and 30 generic tablets using 2 different manual tablet-breaking methods. Group B broke 15 Glynase Prestabs and 15 generic tablets without instructions. Visual analog scales were used to assess pain and difficulty of tablet breaking. RESULTS: A higher percentage of successful tablet breaking was reported with Glynase Prestabs (80%) compared with the generic tablets (33%). Mean pain scores for breaking Glynase Prestabs were 0.1 (Group A) and 0.9 (Group B). Higher pain scores were obtained for the generic tablets (2.1 for Group A, 3.2 for Group B). Glynase Prestabs were easier to break in both groups, and the resultant half tablets showed less variance from the expected theoretical weight (50% of whole parent tablet weight). CONCLUSIONS: Older adults broke Glynase Prestabs more accurately and with less difficulty than generic micronized glyburide tablets. This variation in ease of tablet breaking and accuracy between different tablet formulations affect bioavailability and patient compliance.

Administration, Oral↗
PubMedDate not supplied

Impotence in elderly men.

Impotence is a highly prevalent condition occurring in 10 million American men over the age of 18 years. Alterations in vascular supply, hormonal changes with age, neurological dysfunction and the use of a variety of medications may combine and contribute to impotence. Impotence should not be considered a normal part of the aging process. Careful attention to evaluation for the aetiology of impotence will lead to making appropriate therapeutic choices.

Aged↗
PubMedDate not supplied

Acid hydrolysis of proteins for chromatographic analysis of amino acids.

The conditions used to hydrolyze proteins are vital in determining amino acid compositions because they necessarily represent a compromise aimed at yielding the best estimate of amino acid composition. Variations in ease of peptide bond cleavage, differences in amino acid stabilities, and matrix effects from nonproteinaceous components all militate against a single set of hydrolysis conditions that quantitatively hydrolyze every peptide bond and concurrently cause no destruction of any amino acid. This presentation summarizes and reviews an extensive study which evaluated a number of variations in the techniques and procedures of the classical 6N HCl, 110 degrees C, 24 h hydrolysis of protein. The objectives of the recent investigation were: to compare hydrolysis at 145 degrees C, 4 h with 110 degrees C, 24 h for proteins in a wide range of different sample matrixes; to compare protein hydrolysis at 110 degrees C, 24 h conducted in sealed glass ampoules after vacuum removal of air with hydrolysis in glass tubes with Teflon-lined screw caps after removal of air by vacuum, nitrogen purge, and sonication; to evaluate a performic acid oxidation procedure before hydrolysis for the analysis of cystine and methionine in the different sample matrixes; to evaluate multiple hydrolysis times at 145 degrees C; to evaluate the variation of interlaboratory hydrolysates prepared at 145 degrees C, 4 h in 2 different laboratories on the amino acid analysis of an array of protein-containing matrixes.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗
PubMedDate not supplied

Analysis of amino acids by gas chromatography as the N-trifluoroacetyl n-butyl esters.

This presentation describes amino acid analysis with the gas chromatographic method and experimental conditions using the N-trifluoroacetyl n-butyl ester derivatives; the study we describe here was undertaken to compare gas chromatographic (GC) and ion-exchange chromatographic (IEC) analyses of amino acids in hydrolysates of 9 diverse sample types to gain insight into effects of these 2 chromatographic methods of analysis on variation in amino acid results. Our study showed that values for samples prepared by 2 separate laboratories using the same procedure were generally in good agreement when all of the hydrolysates were analyzed by a single laboratory using a single method of analysis. To compare results from gas chromatography with those from ion-exchange chromatography analyses were performed by 2 different laboratories on the same hydrolysates and on different hydrolysates prepared by the same method by both laboratories. The data demonstrate that GC and IEC can be expected to yield essentially identical results when applied to the same hydrolysate. Agreement is so close that interlaboratory differences in hydrolysate preparation of the same sample contribute as much to variation in amino acid results as does the method of analysis, a fact which should be noted in planning collaborative studies.

Acylation↗