Blood Lactate Responses of Male and Female Players Across an International Rugby Sevens Tournament.

PURPOSE: This study investigated within- and between-matches blood lactate (La-) responses across an international Rugby Sevens tournament (5 matches over 2 d) in male and female players. METHODS: Earlobe blood samples were taken from 25 professional players around matches: before warm-up (PRE), immediately upon finishing match participation (POST), and 30 minutes postmatch (30 min). RESULTS: POST [La-] (mean [SD], range) for males was 10.3 (3.2; 2.9-20.2) mmol·L-1 and for females was 9.1 (2.3; 3.4-14.6) mmol·L-1. Linear mixed-effects models revealed a decrease in POST [La-] after match 5, compared to match 1. Increased PRE [La-] was found before match 2 (+0.8 [0.6-1.1] mmol·L-1), match 3 (+0.8 [0.5-1.1] mmol·L-1), and match 5 (+0.6 [0.4-0.9] mmol·L-1) compared to match 1 (all P < .001). The [La-] remained elevated at 30 min, compared to PRE (+1.7 [1.4-2.0] mmol·L-1, P < .001), with ∼20% of values persisting >4 mmol·L-1. Higher POST was observed in males compared to females (+1.6 [0.1-3.2] mmol·L-1, P = .042); however, no differences between sexes were found across 30 min or PRE [La-]. No [La-] differences between positions (backs and forwards) were identified. CONCLUSIONS: Lactate concentrations above 10 mmol·L-1 are required to effectively simulate the anaerobic demands of international Rugby Sevens matches. Practitioners are advised to individualize anaerobic training prescription due to the substantial variability observed within positional groups. Additionally, improving athletes' metabolic recovery capacity through training, nutrition, and recovery interventions may enhance physical preparation for subsequent matches within a day, where incomplete lactate clearance was observed.

Evidence for the horizontal transfer of an unusual capsular polysaccharide biosynthesis locus in marine bacteria.

The most intensely studied of the Vibrio vulnificus virulence factors is the capsular polysaccharide (CPS). All virulent strains produce copious amounts of CPS. Acapsular strains are avirulent. The structure of the CPS from the clinical isolate ATCC 27562 is unusual. It is serine modified and contains, surprisingly, N-acetylmuramic acid. We identified the complete 25-kb CPS biosynthesis locus from ATCC 27562. It contained 21 open reading frames and was allelic to O-antigen biosynthesis loci. Two of the genes, murA(CPS) and murB(CPS), were paralogs of the murA(PG) and murB(PG) genes of the peptidoglycan biosynthesis pathway; only a single copy of these genes is present in the strain CMCP6 and YJ016 genomes. Although MurA(CPS) and MurB(CPS) were functional when expressed in Escherichia coli, lesions in either gene had no effect on CPS production, virulence, or growth in V. vulnificus; disruption of 8 other genes within the locus resulted in an acapsular phenotype and attenuated virulence. Thus, murA(CPS) and murB(CPS) were functional but redundant. Comparative genomic analysis revealed that while completely different CPS biosynthesis loci were found in the same chromosomal region in other V. vulnificus strains, most of the CPS locus of ATCC 27562 was conserved in another marine bacterium, Shewanella putrefaciens strain 200. However, the average GC content of the CPS locus was significantly lower than the average GC content of either genome. Furthermore, several of the encoded proteins appeared to be of Gram-positive and archaebacterial origin. These data indicate that the horizontal transfer of intact and partial CPS loci drives CPS diversity in marine bacteria.

Picosecond X-ray absorption spectroscopy of a photoinduced iron(II) spin crossover reaction in solution.

In this study, we perform steady-state and time-resolved X-ray absorption spectroscopy (XAS) on the iron K-edge of [Fe(tren(py)3)](PF6)2 dissolved in acetonitrile solution. Static XAS measurements on the low-spin parent compound and its high-spin analogue, [Fe(tren(6-Me-py)3)](PF6)2, reveal distinct spectroscopic signatures for the two spin states in the X-ray absorption near-edge structure (XANES) and in the X-ray absorption fine structure (EXAFS). For the time-resolved studies, 100 fs, 400 nm pump pulses initiate a charge-transfer transition in the low-spin complex. The subsequent electronic and geometric changes associated with the formation of the high-spin excited state are probed with 70 ps, 7.1 keV, tunable X-ray pulses derived from the Advanced Light Source (ALS). Modeling of the transient XAS data reveals that the average iron-nitrogen (Fe-N) bond is lengthened by 0.21+/-0.03 A in the high-spin excited state relative to the ground state within 70 ps. This structural modification causes a change in the metal-ligand interactions as reflected by the altered density of states of the unoccupied metal orbitals. Our results constitute the first direct measurements of the dynamic atomic and electronic structural rearrangements occurring during a photoinduced FeII spin crossover reaction in solution via picosecond X-ray absorption spectroscopy.