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I D Watson

Publications and source records attributed to I D Watson.

83 records · Page 5Linked to original sources

Total body water volumes for adult males and females estimated from simple anthropometric measurements.

Individual total body water volumes for 458 adult males and 265 adult females obtained from dilution studies, together with their height, weight, and age have been selected from the literature. These values were used to derive total body water prediction equations for adults of any age. The equations that gave the best fit were for males: formula (see text) and for females: formula (see text). Numerous other linear regression equations to predict total body water from anthropometric measurements have been reported in the literature. Most apply only to restricted age groups. These, and the equations from the present study were tested on completely independent data. In all cases the equations from the present study gave the best overall results, though for women one equation designed for a specific age group, gave for that age group a marginally better fit.

Adult↗

Assay for trimethoprim in serum and urine by means of ion-pair chromatography.

We describe a rapid, precise, and reliable procedure for assay of trimethoprim in serum and urine by ion-pair chromatography. Trimethoprim concentrations in urine are determined by an externally standardized, direct-injection procedure; assay in serum involves a simple preliminary extraction and internal standardization. The assays are suitable for pharmacokinetic studies and have been applied to determination of trimethoprim concentrations in serum and urine during therapy with Co-trimoxazole, a sulfonamide/trimethoprim preparation.

Chromatography, Gas↗

Obesity indices.

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Adipose Tissue↗

Calorimetric studies of the ADP binding to myosin subfragment 1, heavy meromyosin, and to myosin filaments.

A calorimetric titration method was used to study the ADP binding to the chymotryptic subfragments of myosin, heavy meromyosin (HMM) and myosin subfragment 1 (S-1), and to myosin aggregated into filaments at low ionic strength. The binding constant (K) and heat of reaction (deltaH, kiloJoules (moles of ADP bound)-1) were determined. For HMM in 0.5 M KCl, 0.01 M MgCl2, 0.02 M Tris (pH 7.8) at 12 degrees, log K = 5.92 +/- 0.13 and deltaH = -70.9 +/- 3.6 kJ mol-1. These results agree with our previous findings for myosin in 0.5 M KCl at 12 degrees. When the KCl concentration was reduced to 0.1 M, the binding constant did not change significantly (log K = 6.09 +/- 0.06) but the binding was more exothermic (deltaH = -90.1 +/- 3.3 kJ mol-1). Similar results were obtained for myosin filaments in 0.1 M KCl and also for both the isoenzymes of S-1(S-1(A1) and S-1(A2) in 0.1 M KCl. In 0.5 M KCl, the binding curves suggest that about one ADP is bound per active site, but as 0.1 M KCl, the apparent stoichiometry drops from 0.7 to 0.75. The most probable explanation is that there is some site heterogeneity which is more evident at lower ionic strength.

Adenosine Diphosphate↗