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Biomedical subjects

S H Jackson

Publications and source records attributed to S H Jackson.

At least 109 records · Page 6Linked to original sources
PubMed1978

Specific method for serum creatinine determination based on ion exchange chromatography and an automated alkaline picrate reaction -- a proposed reference method.

A proposed reference method for serum creatinine has been developed under the auspices of the Committee on Reference Methods and Reference Materials of the Canadian Society of Clinical Chemists. A serum ultrafiltrate at pH 2.0 is applied through a closed sample loop injection system to a short column containing cationic resin of high resolving power. Elution with sodium citrate buffer by means of minipump at constant rate passes the eluate into alkaline picrate reagents in a continuous flow system (Technicon AAIII pump, AAII colorimeter 50 mm x 1.5 mm flow cell, narrow band width filter). The colour reaction peak is monitored visually to verify specificity and the area is calculated electronically. Specificity has been demonstrated by use of Jaffé-reactive substances such as glucose, sodium acetoacetate, L-ascorbic acid, pyruvic acid, L-dopa and glycocyamidine and also by use of an alternate colour reaction, sodium 3,5-dinitrobenzoate in place of alkaline picrate in the analysis of serum pools. Routine methods in common use, i.e., manual and automated alkaline picrate procedures, demonstrated a statistically significant high bias in interlaboratory studies in which this procedure was used for reference.

Autoanalysis↗
PubMed1975

Iminodipeptiduria: a genetic defect in recycling collagen; a method for determining prolidase in erythrocytes.

A 39-month-old girl was found to have a genetic deficiency of prolidase. This enzyme specifically splits dipeptides with proline or hydroxyproline at the C-terminus. Absence of the enzyme leads to massive urinary excretion of iminodipeptides. Clinical symptoms include some that can be ascribed to collagen defects. Previously we had demonstrated that the efficient recycling of proline by the breakdown and resynthesis of collagen is a normal physiological process. The collagen defects in this condition could result from interference with the normal recycling of collagen.

Amino Acid Metabolism, Inborn Errors↗
PubMed1975

Proline recycling during collagen metabolism as determined by concurrent 18O2-and 3H-labeling.

In a previous study where rat skin collagen was labeled with 180 in the hydroxyl group of the collagen hydroxyproline we noticed that the decat rate of this label was much faster than had been observed when the skin collagen hydroxyproline was labeled with oH in the prolyl ring. In this study a ratwas labeled concurrently with [1802] and [3H] proline and the rate of decline of both labels was determined in rat skin collagen hydroxyproline. After correction for growth dilution of the skin collagen the [180] hydroxyproline was found to have a half-life of 27 days while the [3H] hydroxyproline had a half-life of 53 days. The decay rate of the [180] hydroxyproline represents the true turnover rate of collagen since there is no possibility of recycling this label. Hence, the difference between this and the [3H] hydroxyproline decay rate is due to recycling of L-[3H] proline into new collagen. The efficiency of recycling of proline from catabolized collagen into new collagen was about 93%.

Animals↗