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Biomedical subjects

M B Clark

Publications and source records attributed to M B Clark.

At least 55 records · Page 3Linked to original sources
PubMed1977

The metabolism of [6-3H]1alpha, hydroxycholecalciferol to [6-3H]1alpha,25-dihydroxycholecalciferol in a patient with renal insufficiency.

To evaluate whether 1alpha-hydroxycholecalciferol is metabolized to 1alpha,25-dihydroxycholecalciferol in man, [6-3H]1alpha-hydroxycholecalciferol was given intravenously to a patient with renal failure who was maintained daily on 100,000 IU vitamin D and calcium supplements. Using Sephadex LH-20 and high-pressure liquid chromatography, it was clearly demonstrated that 1alpha-hydroxycholecalciferol rapidly disappears from the blood and is metabolized to 1alpha,25-dihydroxycholecalciferol.

Dihydroxycholecalciferols↗
PubMed1975

Treatment of hypoparathyroidism and pseudohypoparathyroidism with metabolites of vitamin D: evidence for impaired conversion of 25-hydroxyvitamin D to 1 alpha,25-dihydroxyvitamin D.

In hypoparathyroidism and pseudohypoparathyroidism, pharmacologic doses of vitamin D correct hypocalcemia, but the mechanism is unknown. In two children with hypoparathyroidism and one with pseudohypoparathyroidism we tested the hypothesis that in these conditions there is a defect in synthesis of 1 alpha,25-dihydroxyvitamin D3, the principal active metabolite of vitamin D. In both conditions, minute doses of the metabolite (0.04 to 0.08 mug per kilogram of body weight per day) quickly corrected hypocalcemia and increased intestinal calcium absorption. On the other hand, the effective dose of 25-hydroxyvitamin D3 to maintain normocalcemia was 3 to 4 mug per kilogram per day in the two conditions. Thus, the dosage ratio of 25-hydroxyvitamin D3 to 1 alpha,25-dihydroxyvitamin D3 approximated 100:1. By contrast this ratio was approximately 3:1 in two infants with vitamin D deficiency, a condition in which optimal metabolism of vitamin D would be expected. These findings suggest an impaired conversion of 25-hydroxyvitamin D to 1 alpha,25-dihydroxyvitamin D in both hypoparathyroidism and pseudohypoparathyroidism.

Administration, Oral↗
PubMed1972

Immunochemical studies on human calcitonin M leading to information on the shape of the molecule.

1. Two antisera were obtained from a single rabbit. Both are highly specific for human calcitonin M but react with different parts of the amino acid sequence. 2. The different sequences that react with the antibodies of the two antisera were located. The first antiserum reacts at two sites in the molecule, one in the sequence residues 11-18, probably with residue 17 as the immunodominant group, and another on either side of the 28-29 peptide bond. The second antiserum, harvested 9 months later, reacts principally at one site bridging the 28-29 peptide bond. 3. A consideration of the properties of the hormone's binding sites and of data relating biological activity to structure enables some conclusions to be drawn with regard to the shape of the molecule. It appears that the peptide chain is folded to bring N- and C-termini closer together and that there is non-covalent interaction between regions in the chain near both termini. One of these is located near residue 8.

Amino Acid Sequence↗