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1.
Scand J Med Sci Sports ; 24(4): e290-8, 2014 Aug.
Article in English | MEDLINE | ID: mdl-24397690

ABSTRACT

Sprint (high-intensity) exercise performance is reduced when immediately preceded by cold water immersion (CWI). We aimed to investigate whether this performance effect could be attenuated by combining an active recovery (arm exercise) with hip-level CWI, and whether this attenuation may be related to an effect on core temperature (Tcore ). Participants (n = 8) completed three Wingate tests before (Ex1) and after (Ex2) four different 30-min recovery interventions: CWI at 15 °C (CW15), arm exercise during CWI at 15 °C (CW15+AE), arm exercise during thermoneutral immersion at 34 °C (TW34+AE) and non-immersed arm exercise (AE). After AE and TW34+AE, performance during Ex2 was not different from Ex1; while after CW15+AE and CW15, performance was reduced by 4.9% and 7.6%, respectively. Arm exercise maintained Tcore during recovery in CW15+AE, while it declined to a larger extent upon commencement of Ex2 (-0.9 °C) when compared with CW15 (-0.6 °C). This suggests similar leg muscle cooling during recovery in CW15 and CW15+AE. Without any other significant effects (e.g., on blood lactate), these data suggest that the improvement in sprint performance following an active CWI recovery, over CWI alone, may be related to maintained Tcore and its effect on neurophysiological mechanisms that drive muscle activation, but not by reduced muscle cooling.


Subject(s)
Athletic Performance/physiology , Cryotherapy/methods , Exercise/physiology , Recovery of Function , Adolescent , Adult , Arm/physiology , Body Temperature , Cold Temperature , Exercise Test , Heart Rate , Humans , Immersion , Lactic Acid/blood , Male , Water , Young Adult
2.
Hydrobiologia ; 850(10-11): 2165-2175, 2023.
Article in English | MEDLINE | ID: mdl-37325484

ABSTRACT

The taxonomic status of the zooplanktivorous cichlids Copadichromis mloto and C. virginalis has been confused since their original descriptions by lles in 1960. Whilst two forms of C. virginalis, 'Kaduna' and 'Kajose', were distinguished in the type material, C. mloto has not been positively identified since its original description. Here we re-examined the types as well as 54 recently collected specimens from multiple sampling locations. Genome sequencing of 51 recent specimens revealed two closely related but reciprocally monophyletic clades. Geometric morphological analysis indicated that one clade morphologically encompasses the type specimens of C. virginalis identified by Iles as the Kaduna form, including the holotype, whilst the other clade encompasses not only the paratypes identified as the Kajose form, but also the type series of C. mloto. Given that all three forms in Iles's type series are from the same locality, that there are no meristic or character states to differentiate them and that there are no records of adult male C. mloto in breeding colours, we conclude that the Kajose form previously identified as C. virginalis represents relatively deeper bodied sexually active or maturing individuals of C. mloto. Supplementary Information: The online version contains supplementary material available at 10.1007/s10750-022-05025-1.

3.
Biochemistry ; 40(12): 3710-6, 2001 Mar 27.
Article in English | MEDLINE | ID: mdl-11297439

ABSTRACT

Site-directed mutations were made to the phosphate-binding loop lysine in the beta-subunit of the chloroplast F(1)-ATPase in Chlamydomonas reinhardtii (betaK167) to investigate the participation of this residue in the binding of metal to catalytic site 3 in the absence of nucleotide. The cw-EPR spectra of VO(2+) bound to site 3 of CF(1)-ATPase from wild type and mutants revealed changes in metal ligation resulting from mutations to betaK167. The three-pulse ESEEM spectrum of the wild-type CF(1)-ATPase with VO(2+) bound to site 3 shows an equatorially coordinating (14)N from an amine. The ESEEM spectra of the mutants do not show evidence of an equatorially coordinating amine group. The results presented here show that, in the absence of nucleotide, betaK167 is a ligand to the metal bound at catalytic site 3, suggesting a regulatory role for the P-loop lysine in addition to its known role in catalysis.


Subject(s)
Catalytic Domain , Chlamydomonas reinhardtii/enzymology , Lysine/metabolism , Proton-Translocating ATPases/metabolism , Vanadium/metabolism , Adenosine Diphosphate/metabolism , Adenosine Triphosphate/metabolism , Animals , Binding Sites/genetics , Catalytic Domain/genetics , Chlamydomonas reinhardtii/genetics , Chloroplasts/enzymology , Chloroplasts/genetics , Electron Spin Resonance Spectroscopy , Ligands , Lysine/genetics , Magnesium/metabolism , Mutagenesis, Site-Directed , Oxygen/metabolism , Proton-Translocating ATPases/genetics
4.
Biochemistry ; 39(31): 9393-400, 2000 Aug 08.
Article in English | MEDLINE | ID: mdl-10924134

ABSTRACT

Metal ligands of the VO(2+)-adenosine diphosphate (ADP) complex bound to high-affinity catalytic site 1 of chloroplast F(1) adenosine triphosphatase (CF(1) ATPase) were characterized by electron paramagnetic resonance (EPR) spectroscopy. This EPR spectrum contains two EPR species designated E and F not observed when VO(2+)-nucleotide is bound to site 3 of CF(1). Site-directed mutations betaE197C, betaE197D, and betaE197S in Chlamydomonas CF(1) impair ATP synthase and ATPase activity catalyzed by CF(1)F(o) and soluble CF(1), respectively, indicating that this residue is important for enzyme function. These mutations caused large changes in the (51)V hyperfine tensors of VO(2+)-nucleotide bound to site 1 but not to site 3. Mutations to the Walker homology B aspartate betaD262C, betaD262H, and betaD262T of Chlamydomonas CF(1) caused similar effects on the EPR spectrum of VO(2+)-ADP bound to site 1. These results indicate that the conversion of the low-affinity site 3 conformation to high-affinity site 1 involves the incorporation betaE197 and betaD262 as metal ligands.


Subject(s)
Chlamydomonas reinhardtii/enzymology , Chloroplasts/enzymology , Proton-Translocating ATPases/chemistry , Proton-Translocating ATPases/metabolism , Vanadates/chemistry , Vanadates/metabolism , Adenosine Diphosphate/chemistry , Adenosine Diphosphate/metabolism , Animals , Aspartic Acid/genetics , Binding Sites/genetics , Catalysis , Chlamydomonas reinhardtii/genetics , Chloroplasts/genetics , Electron Spin Resonance Spectroscopy , Glutamic Acid/genetics , Mutagenesis, Site-Directed , Protein Conformation , Proton-Translocating ATPases/genetics , Spin Labels
5.
J Clin Lab Anal ; 10(5): 262-8, 1996.
Article in English | MEDLINE | ID: mdl-8887005

ABSTRACT

A quantitative human immunodeficiency virus type 1 (HIV-1) RNA polymerase chain reaction assay has been validated analytically and clinically in > 13,000 samples. The assay is highly reproducible with intra- and inter-assay precision of 16% and 19%, respectively. In 1,542 of 1,548 subjects with CD4+ counts of 0-500 cells per mm3, viral RNA levels were quantifiable and ranged from approximately 3,000-52,200,000 copies per milliliter. Median plasma HIV-1 RNA values were inversely proportional to CD4+ counts from 0-400 cells per mm3. When patients were off antiretroviral therapies for approximately 14 days prior to the initial baseline RNA PCR evaluation, the mean variance between the two baseline values was 23% (0.1 log). Of these patients, 95% had a sufficient plasma viral load to quantitate a 10-fold (1 log) diminution in viral load caused by antiviral therapy. In contrast, only 20% and 45% of these subjects had sufficient p24 and ICD p24 levels to detect a 50% diminution in circulating virus. The high precision and reproducibility of this quantitative RNA PCR assay provide an enhanced means of evaluating therapeutic drug regimens for HIV-1.


Subject(s)
HIV-1/genetics , Polymerase Chain Reaction , RNA, Viral/blood , Base Sequence , HIV Core Protein p24/blood , Humans , Molecular Sequence Data
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