This study sought to develop a maximal oxygen consumption (VO2max) regression model derived strictly from self-reported non-exercise (N-EX) predictor variables. The VO2max (mean +/- SD; 44.05 +/- 6.6 ml.kg-1.min-1) of 100 physically active college students (50 females, 50 males), aged 18 to 29 yr, was measured using a treadmill protocol and open circuit calorimetry. Questionnaire-based predictor variables used in the N-EX regression model included (a) the subject's perceived functional ability (PFA) to walk, jog, or run given distances, (b) habitual physical activity (PA-R) data, (c) body mass index (BMI), and (d) gender. BMI (kg.m-2) was computed from self-reported body weight in pounds and self-reported body height in feet and inches. The questionnaire-based N-EX regression model (R = 0.85, SEE = 3.44 ml.kg-1.min-1) developed in this study exceeded the accuracy of previously developed N-EX regression models and is comparable to many exercise-based regression models in the literature. Cross-validation using PRESS (predicted residual sum of squares) statistics demonstrated minimal shrinkage (R = 0.84, SEE = 3.60 ml.kg-1.min-1) of the present regression model. The PFA data were useful in explaining observed VO2max variance (squared partial r2 = 0.155, P < 0.0001) and enhanced the ability of the N-EX regression model to accurately predict criterion VO2max. These results suggest that a questionnaire-based N-EX regression model provides a valid and convenient method for predicting VO2max in physically active college students.
Curvilinear fibrils with the tinctorial properties of amyloid were isolated from a patient with bone and joint involvement complicating chronic dialysis for renal disease. Subunit fractions of 24,000 and 12,000 mol wt were identified after gel filtration under dissociating conditions, the latter containing a significant amount of a dimer of the former. This was confirmed by Edman degradation of each fraction, which yielded the amino terminal sequence of normal human beta-2 microglobulin (B2M) to residues 20 and 30, respectively. The size of the subunit protein (12,000 mol wt) and the amino acid composition make it likely that intact B2M is a major constituent of the fibrils. B2M is thus another example of a low molecular weight serum protein, with a prominent beta-pleated sheet structure, that may adopt the fibrillar configuration of amyloid in certain pathologic states.
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