Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 6 de 6
Filter
Add more filters











Database
Language
Publication year range
1.
J Appl Physiol (1985) ; 106(1): 316-25, 2009 Jan.
Article in English | MEDLINE | ID: mdl-18787095

ABSTRACT

During diving, arterial Pco(2) (Pa(CO(2))) levels can increase and contribute to psychomotor impairment and unconsciousness. This study was designed to investigate the effects of the hypercapnic ventilatory response (HCVR), exercise, inspired Po(2), and externally applied transrespiratory pressure (P(tr)) on Pa(CO(2)) during immersed prone exercise in subjects breathing oxygen-nitrogen mixes at 4.7 ATA. Twenty-five subjects were studied at rest and during 6 min of exercise while dry and submersed at 1 ATA and during exercise submersed at 4.7 ATA. At 4.7 ATA, subsets of the 25 subjects (9-10 for each condition) exercised as P(tr) was varied between +10, 0, and -10 cmH(2)O; breathing gas Po(2) was 0.7, 1.0, and 1.3 ATA; and inspiratory and expiratory breathing resistances were varied using 14.9-, 11.6-, and 10.2-mm-diameter-aperture disks. During exercise, Pa(CO(2)) (Torr) increased from 31.5 +/- 4.1 (mean +/- SD for all subjects) dry to 34.2 +/- 4.8 (P = 0.02) submersed, to 46.1 +/- 5.9 (P < 0.001) at 4.7 ATA during air breathing and to 49.9 +/- 5.4 (P < 0.001 vs. 1 ATA) during breathing with high external resistance. There was no significant effect of inspired Po(2) or P(tr) on Pa(CO(2)) or minute ventilation (Ve). Ve (l/min) decreased from 89.2 +/- 22.9 dry to 76.3 +/- 20.5 (P = 0.02) submersed, to 61.6 +/- 13.9 (P < 0.001) at 4.7 ATA during air breathing and to 49.2 +/- 7.3 (P < 0.001) during breathing with resistance. We conclude that the major contributors to increased Pa(CO(2)) during exercise at 4.7 ATA are increased depth and external respiratory resistance. HCVR and maximal O(2) consumption were also weakly predictive. The effects of P(tr), inspired Po(2), and O(2) consumption during short-term exercise were not significant.


Subject(s)
Carbon Dioxide/blood , Diving/adverse effects , Exercise , Hypercapnia/etiology , Prone Position , Respiratory Physiological Phenomena , Adaptation, Physiological , Adult , Airway Resistance , Atmospheric Pressure , Exhalation , Female , Humans , Hypercapnia/blood , Hypercapnia/physiopathology , Immersion , Inhalation , Male , Middle Aged , Models, Biological , Oxygen/blood , Oxygen Consumption , Partial Pressure , Pulmonary Ventilation , Respiratory Dead Space , Risk Factors , Up-Regulation , Young Adult
2.
Glycobiology ; 9(6): 527-32, 1999 Jun.
Article in English | MEDLINE | ID: mdl-10336984

ABSTRACT

Kdn (3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonic acid), a unique deaminated member of the sialic acid family, has emerged as a new building block of glycoconjugates from a wide variety of organisms, ranging from bacteria to mammals. In particular, the presence of Kdn has been demonstrated in different rat organs and tissues, but not in liver. Here we report on the detection and quantitation of Kdn in rat liver and on its variations with postnatal development and aging. We have previously established the optimal conditions for derivatization of Kdn with 1,2-diamino-4, 5-methylene-dioxybenzene (DMB), and detection by reverse-phase HPLC. Analysis of whole liver homogenates and different subcellular fractions reveals that Kdn is fundamentally present in the cytosolic fraction as nucleotide precursor. The expression of Kdn, Neu5Gc, and Neu5Ac changes unevenly with age. While the content of Neu5Ac, the major species, and Neu5Gc decreases to a different extent from newborn to old animals, Kdn content decreases from newborn to trace amounts in adult rats and increases again with aging. Thus, expression of Kdn, Neu5Gc, and Neu5Ac appears to be independently regulated.


Subject(s)
Aging/metabolism , Cytosol/metabolism , Liver/metabolism , Sugar Acids/metabolism , Animals , Chromatography, High Pressure Liquid , Male , Neuraminic Acids/metabolism , Rats , Rats, Wistar , Spectrometry, Fluorescence , Subcellular Fractions/metabolism
3.
FEBS Lett ; 444(2-3): 260-4, 1999 Feb 12.
Article in English | MEDLINE | ID: mdl-10050771

ABSTRACT

PDC-109, the major heparin-binding protein of bull seminal plasma, binds to sperm choline lipids at ejaculation and modulates capacitation mediated by heparin. Affinity chromatography on heparin-Sepharose showed that polydisperse, but not monomeric, PDC-109 displayed heparin-binding capability. We sought to characterise the surface topology of the quaternary structure-dependent heparin-binding region of PDC-109 by comparing the arginine- and lysine-selective chemical modification patterns of the free and the heparin-bound protein. A combination of reversed-phase peptide mapping of endoproteinase Lys-C-digested PDC-109 derivatives and mass spectrometry was employed to identify modified and heparin-protected residues. PDC-109 contains two tandemly arranged fibronectin type II domains (a, Cys24-Cys61; b, Cys69-Cys109). The results show that six basic residues (Lys34, Arg57, Lys59, Arg64, Lys68, and Arg104) were shielded from reaction with acetic anhydride and 1,2-cyclohexanedione in heparin-bound PDC-109 oligomers. In the 1H-NMR solution structures of single fibronectin type II domains, residues topologically equivalent to PDC-109 Arg57 (Arg104) and Lys59 lay around beta-strand D on the same face of the domain. In full-length PDC-109, Arg64 and Lys68 are both located in the intervening polypeptide between domains a and b. Our data suggest possible quaternary structure arrangements of PDC-109 molecules to form a heparin-binding oligomer.


Subject(s)
Heparin/metabolism , Prostatic Secretory Proteins , Protein Conformation , Proteins/chemistry , Semen/chemistry , Acetic Anhydrides/metabolism , Amino Acid Sequence , Animals , Arginine/metabolism , Cattle , Cyclohexanones/metabolism , Fibronectins/chemistry , Lysine/metabolism , Magnetic Resonance Spectroscopy , Mass Spectrometry , Metalloendopeptidases , Models, Molecular , Molecular Sequence Data , Peptide Mapping , Protein Binding , Protein Structure, Secondary , Seminal Plasma Proteins , Sequence Alignment
4.
Appl Opt ; 34(24): 5312-25, 1995 Aug 20.
Article in English | MEDLINE | ID: mdl-21060350

ABSTRACT

We describe the design and performance of large-aperture (>30 cm × 30 cm) optical switches that have demonstrated, for the first time to our knowledge, active switching of a high-energy (>5 kJ) optical pulse in an inertial-confinement fusion laser. These optical switches, which consist of a plasma-electrode Pockels cell (PEPC) and a passive polarizer, permit the design of efficient, multipass laser amplifiers. In a PEPC, plasma discharges on the faces of a thin (1-cm) electro-optic crystal (KDP or KD*P) act as highly conductive and transparent electrodes. These plasma electrodes facilitate rapid (<100 ns) and uniform charging of the crystal to the half-wave voltage and discharging back to 0 V. We discuss the operating principles, design, optical performance, and technical issues of a 32 cm × 32 cm prototype PEPC with both KDP and KD*P crystals, and a 37 cm × 37 cm PEPC with a KDP crystal for the Beamlet laser. This PEPC recently switched a 6-kJ, 3-ns pulse in a four-pass cavity.

SELECTION OF CITATIONS
SEARCH DETAIL