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1.
Int J Sports Med ; 28(9): 732-5, 2007 Sep.
Article in English | MEDLINE | ID: mdl-17525882

ABSTRACT

This study examined the concentrations and the relationships of soluble leptin receptor (sLR) and leptin levels among both physically active people and lean sedentary persons. Information collected for this study came from twelve joggers (JOG), ten weight trainers (WET) and eleven lean sedentary persons (CON). Regular exercisers were defined as those who consistently participated in jogging or weight training 30 minutes a day, at least four times a week, for a period of no less than three years prior to the study. The CON group was defined as exercising, at most, one time per week, less than 20 minutes each time if at all. Leptin and sLR were analyzed using enzyme-linked immunosorbent assay. The results show the BMI of the WET group to be higher than the other groups, yet their percent body fat was not significantly different. Although sLR levels of the JOG group were higher than the WET and CON groups, their free leptin index (FLI) did not show a significant difference. The sLR levels for joggers were higher than the weight trainers. The sLR concentration or the ratio of sLR to fat mass may be an alternative index to FLI for comparing physically active and lean people.


Subject(s)
Exercise/physiology , Leptin/physiology , Receptors, Leptin/physiology , Adult , Body Composition , Female , Health Surveys , Humans , Male , Running/physiology , Surveys and Questionnaires , Weight Lifting/physiology
2.
Theor Appl Genet ; 71(2): 263-7, 1985 Dec.
Article in English | MEDLINE | ID: mdl-24247392

ABSTRACT

A method was worked out using trifluoromethanesulfonic acid (TFMS) as a reagent to split the covalently bound proteins, which are NaCl insoluble, from pollen tube walls of Lilium longiflorum, leaving the peptide bonds essentially intact. After electrophoretic separation, comparisons were made among these proteins from pollen grains and pollen tubes grown in vitro and in styles after self- and cross-pollination. It was found that a) the patterns of covalently bound wall proteins were different between tubes grown in vitro and in vivo; b) fewer bands were found in covalently bound wall proteins than that in noncovalently bound proteins; c) the bands remained almost the same no matter whether the tubes had been cross pollinated or self pollinated, indicating that while the noncovalently bound proteins were involved in incompatibility as shown in the previous paper, the covalently bound proteins may only serve as a structural component, having little to do with incompatibility.

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