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1.
J Sports Sci ; 18(9): 751-8, 2000 Sep.
Article in English | MEDLINE | ID: mdl-11043900

ABSTRACT

This study used a quasi-applied research model to identify and develop potentially talented female soccer players. Athletes aged 15-19 years with a background in team ball sports or athletics were targeted for recruitment using advertisements and promotions through various media. Interested athletes attended a 2-day programme of testing, which included assessment of anthropometric, physiological and skill attributes. A combination of factors was used in the final selection of 17 athletes to take part in a 12-month talent development programme. A pre-season programme of five training sessions per week was conducted for 2 months. This programme focused on enabling the players to acquire the necessary ball and game skills to perform competitively in a short time. The squad competed as a team in the reserve grade competition of an Australian state league. At the conclusion of the 25-game season, 10 players were selected for zone teams with two players progressing to state team selection within 6 months. The project demonstrates that it is possible to select potential female soccer players based on anthropometric, physiological and skill attributes. Selection procedures could be enhanced through the development of objective assessment tools that measure tactical and technical competence. Programmes such as this can offer an additional avenue of player recruitment in support of existing procedures.


Subject(s)
Motor Skills/physiology , Physical Education and Training/organization & administration , Soccer/education , Soccer/physiology , Adolescent , Adult , Anthropometry , Female , Humans , Program Development , Queensland
2.
J Sci Med Sport ; 3(4): 391-405, 2000 Dec.
Article in English | MEDLINE | ID: mdl-11235005

ABSTRACT

Talent identification programs have traditionally focused on individual sports with discrete physical and physiological characteristics. Limited attention has been directed toward predicting performance in team sports. This study measured anthropometric and physiological attributes of 125 male and 123 female junior basketball players competing at the Australian Under 16 championships in 1998. In addition, experienced coaches rated the performance of players during the championships. Performance profiles were compared across playing positions and by playing performance ('Best versus Rest'). Differences in anthropometric characteristics were present across some playing positions for both males and females. Speed and agility differences between some playing positions were also present. Best players differed to Rest players on a number of anthropometric and physiological variables for both males and females. Regression analyses indicated the test variables accounted for a significant proportion of variance in playing performance for both females (41.3%) and males (38.3%). A Z score analysis indicated good alignment between the test and coach ranking of the Best player in four out of five positions for females and two out of five positions for males. Anthropometric and physiological profiling can contribute to selection procedures in junior basketball, however determinants of success are multi-factorial.


Subject(s)
Anthropometry , Basketball/physiology , Exercise/physiology , Physical Fitness/physiology , Adolescent , Analysis of Variance , Female , Humans , Male , Predictive Value of Tests , Regression Analysis , Sampling Studies , Sensitivity and Specificity , Sex Factors
3.
Eur J Biochem ; 66(1): 85-93, 1976 Jun 15.
Article in English | MEDLINE | ID: mdl-954747

ABSTRACT

Br- has been used as a nuclear magnetic resonance (NMR) probe to study the reversible association of alpha-chymotrypsin and an Hg-labelled substrate (4-bromomercuriocinnamic acid, BrHgCin) which rapidly exchanges Br-. T1 was measured for 79Br and 81Br, using a pulse spectrometer. Values of the parameters that determine T1, Obs in aqueous solutions of KBr (pH=5.5) containing alpha-chymotrypsin and BrHgCin are reported. It is found that the rate of Br exchange is diffusion-limited and faster than the rate of reorientation of the BrHgCin-alpha-chymotrypsin complex. The rate constant for the formation of the covalent BrHgCin-alpha-chymotrypsin complex determined by this technique agrees well with previously published data. The rapid rate of Br exchange with the complex, however, is incompatible with the side chain of BrHgCin being entirely buried in a nonpolar pocket on the enzyme but compatible with the side chain being exposed to the solution. The contribution to the NMR signal from the non-covalent complex is negligible.


Subject(s)
Bromine , Chymotrypsin , Organometallic Compounds , Binding Sites , Chymotrypsin/metabolism , Cinnamates , Isotopes , Kinetics , Magnetic Resonance Spectroscopy , Mathematics , Molecular Conformation , Organomercury Compounds , Organometallic Compounds/metabolism , Protein Binding , Protein Conformation
4.
Vox Sang ; 30(1): 23-35, 1976.
Article in English | MEDLINE | ID: mdl-1251568

ABSTRACT

The lecithin:cholesterol acyltransferase (LCAT) activity and lysolecithin content of human blood stored under standard blood transfusion service conditions at 4 degrees C for 6 weeks has been investigated. Cooling the blood to 4 degrees C rapidly inactivates the LCAT reaction, but the enzyme is not denatured during storage under these conditions. Citrate in the anticoagulant did not activate the LCAT reaction in freshly-taken whole blood. The total phospholipid and total lysolecithin content of whole blood decreased during storage at 4 degrees C for 6 weeks. The lysolecithin content of fresh red cells (2.0-3.0 mumol lysolecithin x 10(-11) per cell) showed no significant change during the storage period.


Subject(s)
Acyltransferases/blood , Blood Preservation/methods , Erythrocyte Aging , Lysophosphatidylcholines/blood , Phosphatidylcholine-Sterol O-Acyltransferase/blood , Blood Banks , Citrates/pharmacology , Humans , Phospholipids/blood , Time Factors
10.
J Physiol ; 221(2): 311-29, 1972 Mar.
Article in English | MEDLINE | ID: mdl-5020980

ABSTRACT

1. Data on the transport of L-leucine into human erythrocytes at 25 degrees C shows (a) that the carrier re-orientation process is rate determining, (b) that the binding of leucine to the carrier increases the rate of carrier re-orientation and (c) that the carrier is, at equilibrium, about equally distributed between the membrane surfaces at 25 degrees C.2. These conclusions are reached through a new kinetic analysis of a simple carrier system, which involves no prior assumptions about the relative magnitudes of the rate constants, yet leads to usable kinetic equations. These equations allow the determination of the rate determining step, the calculation of the effect of bound substrate on the rate of carrier re-orientation and, in some cases, an estimate to be made of the equilibrium distribution of the carrier between the inner and outer membrane surfaces.


Subject(s)
Erythrocytes/metabolism , Leucine/metabolism , Binding Sites , Biological Transport, Active , Carbon Isotopes , Cell Membrane , Humans , In Vitro Techniques , Kinetics , Temperature
11.
J Physiol ; 221(2): 331-48, 1972 Mar.
Article in English | MEDLINE | ID: mdl-5020981

ABSTRACT

1. Experiments are reported on the entry, exit and exchange fluxes of L-leucine in human erythrocytes in the temperature range 0-37 degrees C. The kinetics of entry and exit become quite different at low temperatures, indicating an asymmetry in the transport mechanism.2. The data is analysed in terms of a simple carrier mechanism. This shows that carrier re-orientation is rate determining at all temperatures studied, and suggests, although does not prove, that the origin of the asymmetry of the carrier may be an unequal equilibrium distribution of the carriers between inward and outward orientations.3. The activation energy increases sharply on going to low temperatures. This increase is the sum of two components. One arises from differences between the activation energies for inward and outward carrier re-orientations, and the other from changes, with temperature, in the activation energies of the individual carrier re-orientation steps.


Subject(s)
Erythrocytes/metabolism , Leucine/metabolism , Temperature , Activation Analysis , Binding Sites , Biological Transport, Active , Carbon Isotopes , Humans , In Vitro Techniques , Kinetics
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