SEARCH · PubMed Health

Results for “PSOAS MUSCLE”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 469 records · Page 26Linked to original sources

PubMed1992

Contraction of glycerinated rabbit slow-twitch muscle fibers as a function of MgATP concentration.

We have measured the isometric tension and force-velocity relationships of glycerinated rabbit slow-twitch semimembranosus muscle as a function of MgATP concentration ([MgATP]) and have compared the results with those obtained previously from fast-twitch psoas muscle. We find that isometric tension decreases as [MgATP] increases. The magnitude of the decrease is not as great as observed in psoas. Maximum shortening velocity (Vmax) exhibits classical Michaelian saturation behavior with respect to [MgATP] with a Michaelis constant (Km) for half-maximal velocity of 18 microM and a value at saturating [MgATP] of 0.6 muscle lengths/s. Similar values were observed in fibers from soleus, another slow-twitch muscle. The corresponding values in rabbit psoas muscle are 150 microM and 1.6 lengths/s. Compared with psoas, in semimembranosus muscle Km decreases by a factor of approximately 10, whereas Vmax decreases by about a factor of 3. Thus, although in a nonphysiological regime, at low [MgATP], a "fast" muscle actually has a lower shortening velocity than a "slow" muscle.

Adenosine Triphosphate↗

PubMed1993

The role of catecholamines in muscular growth.

This paper reports on an experiment concerning the involvement of catecholamines in the biosynthesis of nucleic acids and proteins at muscular levels, using various types of skeletal muscles (psoas, diaphragm, soleus) and heart muscles from male Wistar rats treated with adrenalin. Assessment of the biosynthetic processes was made by the uptake level of 3H thymidine, 3H uridine, and 3H triptophan in the muscles. The experiment showed the followings: a) nucleic acids and protein synthesis stayed unchanged in the psoas; b) adrenalin stimulated the uptake of the radioactive precursors in the diaphragm and soleus, and c) the biosynthetic processes were inhibited in the myocardium by adrenalin administration. Though adrenalin is known to stimulate proteic synthesis in the skeletal muscle, our study showed that this process occurs only in certain types of muscles (with slow contraction). Inhibition of proteic synthesis in the myocardium in the presence of adrenalin might be one of the cellular mechanisms involved in cardiac failure.

Animals↗

PubMed1996

Spectral analysis of muscle fiber images as a means of assessing sarcomere heterogeneity.

A new image-analysis-based method is described for assessing sarcomere heterogeneity in skinned rabbit psoas muscle fiber segments. This method consists of off-line, two-dimensional Fourier spectral analysis of video-taped muscle images. Local sarcomere length is assessed by partitioning the muscle images into half and quarter images spanning the original image and analyzing the associated spectra. The spectra are analyzed in two different ways, yielding two measures of sarcomere length. The first measure is obtained by calculating and inverting the centroid frequency of the first-order peak associated with each two-dimensional Fourier spectrum. The second measure is obtained in a similar manner, the only difference being that the two-dimensional spectra are first collapsed into one-dimensional line spectra by summing the pixels perpendicular to the fiber axis. Comparison of the two measures provides a measure of striation skewness that cannot be obtained by other image analysis based methods that determine sarcomere length by analyzing selected line luminance profiles.

Animals↗

PubMed1999

Effects of inorganic phosphate on endothermic force generation in muscle.

Using a rapid (ca. 0.2 ms) laser temperature jump technique, the rate of endothermic force generation was examined in single-skinned (rabbit psoas) muscle fibres when they were exposed to different levels of inorganic phosphate (a product released during ATP hydrolysis in active muscle). The steady force is reduced by increased phosphate but the apparent rate constant of force generation induced by a standard temperature jump (from ca. 9 degrees C to ca. 12 degrees C) increases two- to threefold when the phosphate added is increased from zero to ca. 25 mM. The increase in the apparent rate constant also exhibits saturation at higher phosphate levels and the relation is hyperbolic. Detailed examination of the data, particularly in relation to our pressure release experiments, leads to a scheme for the molecular steps involved in phosphate release and force generation in active muscle fibres, where phosphate release from attached cross-bridges involves three reversible and sequentially faster molecular steps. Step one is a moderately slow, pre-force generation step that probably represents a transition of cross-bridges from non-specific to stereospecific attached states. Step two is moderately fast and represents endothermic cross-bridge force generation (temperature sensitive) and step three is a very rapid phosphate release. Such a scheme accommodates findings from a variety of different studies, including pressure perturbation experiments and other studies where the effect of phosphate on muscle force was studied.

Animals↗

PubMed2004

Light microscopy and image analysis of thin filament lengths utilizing dual probes on beef, chicken, and rabbit myofibrils.

Image analysis procedures for immunofluorescence microscopy were developed to measure muscle thin filament lengths of beef, rabbit, and chicken myofibrils. Strips of beef cutaneous trunci, rectus abdominis, psoas, and masseter; chicken pectoralis; and rabbit psoas muscles were excised 5 to 30 min postmortem. Fluorescein phalloidin and rhodamine myosin subfragment-1 (S1) were used to probe the myofibril structure. Digital images were recorded with a cooled charge-coupled device controlled with IPLab Spectrum software (Signal Analytics Corp.) on a Macintosh operating system. The camera was attached to an inverted microscope, using both the phase-contrast and fluorescence illumination modes. Unfixed myofibrils incubated with fluorescein phalloidin showed fluorescence primarily at the Z-line and the tips of the thin filaments in the overlap region. Images were processed using IPLab and the National Institutes of Health's Image software. A region of interest was selected and scaled by a factor of 18.18, which enlarged the image from 11 pixels/microm to approximately 200 pixels/microm. An X-Y plot was exported to Spectrum 1.1 (Academic Software Development Group), where the signal was processed with a second derivative routine, so a cursor function could be used to measure length. Fixation before phalloidin incubation resulted in greatest intensity at the Z lines but a more-uniform staining over the remainder of the thin filament zone. High-resolution image capture and processing showed that thin filament lengths were significantly different (P < 0.01) among beef, rabbit, and chicken, with lengths of 1.28 to 1.32 microm, 1.16 microm, and 1.05 microm, respectively. Measurements using the S1 signal confirmed the phalloidin results. Fluorescent probes may be useful to study sarcomere structure and help explain species and muscle differences in meat texture.

Actin Cytoskeleton↗

PubMedDate not supplied

Analysis of nucleotide myosin complexes in skeletal muscle fibres by DSC and EPR.

The internal dynamics and thermal unfolding of fibre bundles prepared from rabbit psoas muscle has been studied in the presence of nucleotides by differential scanning calorimetry (DSC) and electron paramagnetic resonance (EPR) spectroscopy. Using ADP, adenosine 5'-triphosphate (ATP), AMP.PNP and inorganic phosphate analogue orthovanadate (V(i)), AlF(4)(-) and BeF(3)(-), three intermediate states of the ATP hydrolysis cycle were simulated in glycerinated muscle fibres. In the main transition of the DSC pattern, three overlapping endotherms were detected in rigor, four in strongly as well as weakly binding state of myosin to actin. Deconvolution procedure showed that the transition temperature of 67.5 degrees C was the same for rigor and strong binding state of myosin. In contrast, nucleotide binding induced shift of the melting temperatures of 52 degrees C and 67.5 degrees C, appeared a new fourth peak at 74 and 77 degrees C and produced changes in the calorimetric enthalpies. The changes of the parameters of the peak functions suggest global rearrangements of the internal structure in myosin heads in the intermediate states. In the presence of ADP or ATP plus phosphate analogue orthovanadate or beryllium fluoride, aluminium fluoride, the conventional EPR spectra of spin-labeled muscle fibres showed large changes in the ordering of the probe molecules, and a new distribution of spin labels appeared. ATP plus orthovanadate induced the orientation disorder of myosin heads; the random population of spin labels gave evidence of large local conformational and motional changes in the internal structure of myosin heads. Saturation transfer EPR measurements reported increased rotational mobility of spin labels in the presence of ATP plus phosphate analogues corresponding to weakly binding state of myosin to actin.

Actins↗

PubMed1999

Glycogen synthase kinase-3 is the predominant insulin-regulated eukaryotic initiation factor 2B kinase in skeletal muscle.

Eukaryotic initiation factor eIF2B is a guanine nucleotide exchange protein involved in regulation of translation initiation. Phosphorylation of the epsilon-subunit is thought to be important in insulin-mediated changes in eIF2B activity. However, elucidation of insulin's action has proven elusive, primarily because eIF2B epsilon is a substrate in vitro for at least three different protein kinases. In the present study, we observed changes in eIF2B epsilon kinase activity only in those muscles previously shown to exhibit alterations in protein synthesis in response to insulin. Specifically, eIF2B epsilon kinase activity was increased in psoas muscle from diabetic rats compared to controls. Treating diabetic rats with insulin rapidly reduced eIF2B epsilon kinase activity below control values. Changes were not observed in heart. To identify the kinase(s) in psoas responsible for phosphorylating eIF2B epsilon, the wildtype and two variant forms of the epsilon-subunit were expressed in and purified from Sf9 insect cells, and were used as substrates in protein kinase assays. The first variant contained a point mutation in the eIF2B epsilon cDNA that converted the glycogen synthase kinase-3 (GSK-3) phosphorylation site, Ser535, to a nonphosphorylatable Ala residue. In the second variant, the putative GSK-3 'priming' site, Ser539, was converted to Asp. Based on the pattern of phosphorylation of the wildtype and two variant forms of eIF2B epsilon using casein kinase (CK)-I, CK-II, or GSK-3 as well as that observed with skeletal muscle extracts, we conclude that the predominant eIF2B epsilon kinase in psoas muscle is GSK-3. Thus, insulin-mediated changes in eIF2B activity are likely to involve GSK-3.

Amino Acid Sequence↗

PubMed1996

Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscle.

The orientation of the light-chain region of myosin heads in relaxed, rigor, and isometrically contracting fibers from rabbit psoas muscle was studied by fluorescence polarization. Cysteine 108 of chicken gizzard myosin regulatory light chain (cgRLC) was covalently modified with iodoacetamidotetramethylrhodamine (iodo-ATR). Native RLC of single glycerinated muscle fibers was exchanged for labeled cgRLC in a low [Mg2+] rigor solution at 30 degrees C. Troponin and troponin C removed in this procedure were replaced. RLC exchange had little effect on active force production. X-ray diffraction showed normal structure in rigor after RLC exchange, but loss of axial and helical order in relaxation. In isolated myofibrils labeled cgRLC was confined to the regions of the sarcomere containing myosin heads. The ATR dipoles showed a preference for orientations perpendicular to the fiber axis, combined with limited nanosecond rotational motion, in all conditions studied. The perpendicular orientation preference was more marked in rigor than in either relaxation or active contraction. Stretching relaxed fibers to sarcomere length 4 microns to eliminate overlap between actin- and myosin-containing filaments had little effect on the orientation preference. There was no change in orientation preference when fibers were put into rigor at sarcomere length 4.0 microns. Qualitatively similar results were obtained with ATR-labeled rabbit skeletal RLC.

Animals↗

PubMed1995

Enhancing effect of calmodulin on Ca(2+)-induced Ca2+ release in the sarcoplasmic reticulum of rabbit skeletal muscle fibres.

1. We analysed the effect of calmodulin on Ca(2+)-induced Ca2+ release (CICR) in the sarcoplasmic reticulum (SR) using chemically skinned fibres of rabbit psoas muscle. Ca2+ release was measured using fura-2 microfluorometry. 2. In saponin-skinned fibres, calmodulin potentiated Ca2+ release at low Ca2+ concentrations (< 3 microM), while it showed an inhibitory effect at high Ca2+ concentrations (3-30 microM). 3. Co-application of ryanodine and calmodulin at 0.3 microM Ca2+, but not ryanodine alone, induced a decline in the Ca2+ uptake capacity of the SR, an effect expected from the open-lock of active CICR channels by ryanodine. Thus, potentiation of Ca2+ release by calmodulin at low Ca2+ concentrations can be regarded as a result of the activation of the ryanodine receptor. 4. Greater concentrations of calmodulin were required for potentiation of CICR at low Ca2+ concentrations (1 microM) than for inhibition at high Ca2+ concentrations (10 microM). 5. In beta-escin-permeabilized fibres in which intrinsic calmodulin was retained, the rates of CICR were similar to those measured in the presence of 1 microM calmodulin in saponin-permeabilized fibres. 6. These results suggest that calmodulin plays an important role in the regulation of CICR channels in intact skeletal muscle fibres.

Animals↗

PubMed1996

Psoas sheath chemical neurolysis for management of intractable leg pain from metastatic liposarcoma.

CASE REPORT: A 56-year-old man with widely metastatic liposarcoma, after left Tower extremity amputation, complained of severe right lower extremity pain. Trials of systemic opioids had resulted in poor pain control while introducing intolerable dose-limiting side effects. METHODS AND RESULTS: Initial inpatient management consisted of a lumbar epidural infusion of a dilute local anesthetic and preservative-free morphine. This provided satisfactory relief but was discontinued because of recrudescence of phantom limb pain. A lumbar epidural infusion of preservative-free morphine sulfate was associated with poor pain relief, central nervous system (CNS) side effects, and severe urinary retention resulting in acute renal failure. A repeated trial of parental opioids provided marginal pain relief with persistent CNS side effects. Chemical neurolysis of the lumbar plexus was performed with 10 ml of 10% aqueous phenol injected into the psoas muscle sheath. The pain gradually resolved over a 2-day period without apparent side effects. Motor function was preserved, pain was resolved, and as systemic opioids were reduced, cognitive function and overall well-being were improved.

Amputation, Surgical↗

PubMed1996

Tensile strength and dilatational elasticity of giant sarcolemmal vesicles shed from rabbit muscle.

1. Mechanical properties of the surface membrane of skeletal muscle were determined on sarcolemmal vesicles (mean diameter, 71 microns) shed by rabbit psoas muscle swelling in 140 mM KC1 containing collagenase. 2. Vesicles were stressed by partial aspiration into parallel bore pipettes. The isotropic membrane tension so created caused an increase in membrane area which expresses itself in an elongation of the vesicle projection into the pipette. 3. For individual vesicles, a linear relationship between membrane tension and membrane area increase was found up to the point when the vesicle burst, i.e. sarcolemmal vesicles behaved as perfectly elastic structures. 4. The maximum tension sarcolemmal vesicles could sustain before bursting was 12.4 +/- 0.2 mN m-1 (median +/- 95% confidence interval), and the corresponding fractional increase in membrane area was 0.026 +/- 0.005 (median +/- 95% confidence interval). The elastic modulus of area expansion was 490 +/- 88 mN m-1 (mean +/- S.D.). 5. In conformity with cited comparable work on red blood cells and artificial lipid vesicles, the strength and area elasticity of the skeletal muscle membrane are considered properties of the fluid lipid matrix of the membrane and of the degree to which the bilayer is perturbed by lipid-protein interaction.

Animals↗

PubMed1997

Effect of psoas training on postmenopausal lumbar bone loss: a 3-year follow-up study.

The present study completed a previous randomized trial that demonstrated the protective effect of 1-year psoas training on lumbar bone loss in postmenopausal women. Computerized tomography had been carried out at the beginning (CT1) and at the end (CT2) of this trial. In the present study, 67 women having completed the first trial were asked to practice psoas exercises (60 hip flexions in sitting position with a 5 kg weight on the knee) for 2 additional years with a third CT control at the end of this period (CT3). The aim of this complementary study was to assess the compliance rate and long-term effect on bone of daily psoas muscle training over a longer period. Twenty-one women performed this daily psoas training for 3 years from CT1 to CT3, and 14 acted as controls during the same period. Fourteen women were controls during the first year (from CT1 to CT2) but practiced psoas training during the following 2 years (from CT2 to CT3). Four women were psoas trained during the first year (from CT1 to CT2) and subsequently crossed over to the control group for the last 2 years. The compliance rate was 42%, with an attendance rate of 88%. The lumbar bone loss was lower in the 21 women trained over the 3 years (-3.26 +/- 28.45 mg/cm3) than in the 14 untrained women (-16.79 +/- 8.51 mg/cm3) (P = 0.02). The bone loss was not significantly reduced between the two periods of the study in the 12 women having been controls from CT1 to CT2 and having crossed over to the active training group from CT2 to CT3. Psoas training may be effective against lumbar bone loss. We conclude that specific training may play a contributing role in the preventive strategy to avoid osteoporosis.

Anthropometry↗

PubMed1997

ATPase kinetics on activation of rabbit and frog permeabilized isometric muscle fibres: a real time phosphate assay.

1. The rate of appearance of inorganic phosphate (Pi) and hence the ATPase activity of rabbit psoas muscle in single permeabilized muscle fibres initially in rigor was measured following laser flash photolysis of the P3-1-(2-nitrophenyl)ethyl ester of ATP (NPE-caged ATP) in the presence and absence of Ca2+. Pi appearance was monitored from the fluorescence signal of a Pi-sensitive probe, MDCC-PBP, a coumarin-labelled A197C mutant of the phosphate-binding protein from Escherichia coli. Fibres were immersed in oil to optimize the fluorescence signal and to obviate diffusion problems. The ATPase activity was also measured under similar conditions from the rate of NADH disappearance using an NADH-linked coupled enzyme assay. 2. On photolysis of NPE-caged ATP in the presence of Ca2+ at 20 degrees C, the fluorescence increase of MDCC-PBP was non-linear with time. ATPase activity was 41 s-1 in the first turnover based on a myosin subfragment 1 concentration of 150 microM. This was calculated from a linear regression of the fluorescence signal reporting 20-150 microM of Pi release. Tension was at 67% of its isometric level by the time 150 microM Pi was released. ATPase activities were 36 and 31 s-1 for Pi released in the ranges of 150-300 microM and 300-450 microM, respectively. The ATPase activity had a Q10 value of 2.9 based on measurements at 5, 12 and 20 degrees C. 3. An NADH-linked assay showed the ATPase activity had a lower limit of 12.7 s-1 at 20 degrees C. The response to photolytic release of ADP showed that the rate of NADH disappearance was partially limited by the flux through the coupled reactions. Simulations indicated that the linked assay data were consistent with an initial ATPase activity of 40 s-1. 4. On photolysis of NPE-caged ATP in the absence of Ca2+ the ATPase activity was 0.11 s-1 at 20 degrees C with no discernible rapid transient phase of Pi release during the first turnover of the ATPase. 5. To avoid the rigor state, the ATPase rate in the presence of Ca2+ was also measured on activation from the relaxed state by photolytic release of Ca2+ from a caged Ca2+ compound, nitrophenyl-EGTA. At 5 degrees C the ATPase rate was 5.8 and 4.0 s-1 in the first and second turnovers, respectively. These rates are comparable to those when NPE-caged ATP was used. 6. The influence of ADP and Pi on the ATPase activities was measured using the MDCC-PBP and NADH-linked assays, respectively. ADP (0.5 mM) decreased the initial ATPase rate by 23%. Pi (10 mM) had no significant effect. Inhibition by ADP, formed during ATP hydrolysis, contributed to the decrease of ATPase activity with time. 7. The MDCC-PBP assay and NPE-caged ATP were used to measure the ATPase rate in single permeabilized muscle fibres of the semitendinosus muscle of the frog. At 5 degrees C in the presence of Ca2+ the ATPase activity was biphasic being 15.0 s-1 during the first turnover (based on 180 microM myosin subfragment 1). Tension was 74% of its isometric level by the time 180 microM Pi was released. During the third turnover the ATPase rate decreased to about 20% of that during the first turnover. 8. ATPase activity in isometric rabbit muscle fibres during the first few turnovers is about an order of magnitude greater than that when a steady state is reached. Possible reasons and the consequences for understanding the mechanism of muscular contraction are discussed.

Actin Cytoskeleton↗

PubMed1996

Effects of phosphate and ADP on shortening velocity during maximal and submaximal calcium activation of the thin filament in skeletal muscle fibers.

The effects of added phosphate and MgADP on unloaded shortening velocity during maximal and submaximal Ca2+ activation of the thin filament were examined in skinned single skeletal fibers from rabbit psoas muscle. During maximal Ca2+ activation, added phosphate (10-30 mM) had no effect on unloaded shortening velocity as determined by the slack-test technique. In fibers activated at submaximal concentrations of Ca2+ in the absence of added phosphate, plots of slack length versus duration of unloaded shortening were biphasic, consisting of an initial high velocity phase of shortening and a subsequent low velocity phase of shortening. Interestingly, in the presence of added phosphate, biphasic slack-test plots were no longer apparent. This result was obtained in control fibers over a range of submaximal Ca2+ concentrations and in maximally Ca2+ activated fibers, which were first treated to partially extract troponin C. Thus, under conditions that favor the appearance of biphasic shortening (i.e., low [Ca2+], troponin C extraction), added phosphate eliminated the low velocity component. In contrast, in fibers activated in the presence of 5 mM added MgADP, biphasic slack-test plots were apparent even during maximal Ca2+ activation. The basis of biphasic shortening is not known but it may be due to the formation of axially compressed cross-bridges that become strained to bear a tension that opposes the relative sliding of the myofilaments. The present findings could be explained if added phosphate and MgADP bind to cross-bridges in a strain-dependent manner. In this case, the results suggest that phosphate inhibits the formation of cross-bridges that bear a compressive strain. Added MgADP, on the other hand, may be expected to detain cross-bridges in strong binding states, thus promoting an increase in the population of cross-bridges bearing a compressive strain. Alterations in the population of strained cross-bridges by added phosphate and MgADP would alter the internal load within the fiber and thus affect the speed of fiber shortening.

Actomyosin↗

PubMed1986

Tension responses of muscle to n-step pseudo-random length reversals: a frequency domain representation.

A high resolution, time efficient method is described for determining the complex modulus of activated striated muscle. In this method the applied oscillation of muscle length takes the form of pseudo-random binary noise, PRBN. As a time-domain signal, PRBN is an extension of the double step approach to include n steps; as a frequency-domain signal, PRBN has the properties of quasi-white noise. Fourier analysis of the PRBN length oscillations and the resulting interrupted tension transients gives rise to the complex modulus values. PRBN provides a practical demonstration of the conceptual link between time and frequency domain descriptions of strain sensitive dynamics. The method is demonstrated with intact rat papillary muscle, and glycerol extracted rabbit psoas muscle.

Animals↗

PubMed1990

Hydrostatic compression in glycerinated rabbit muscle fibers.

Glycerinated muscle fibers isolated from rabbit psoas muscle, and a number of other nonmuscle elastic fibers including glass, rubber, and collagen, were exposed to hydrostatic pressures of up to 10 MPa (100 Atm) to determine the pressure sensitivity of their isometric tension. The isometric tension of muscle fibers in the relaxed state (passive tension) was insensitive to increased pressure, whereas the muscle fiber tension in rigor state increased linearly with pressure. The tension of all other fiber types (except rubber) also increased with pressure; the rubber tension was pressure insensitive. The pressure sensitivity of rigor tension was 2.3 kN/m2/MPa and, in comparison with force/extension relation determined at atmospheric pressure, the hydrostatic compression in rigor muscle fibers was estimated to be 0.03% Lo/MPa. As reported previously, the active muscle fiber tension is depressed by increased pressure. The possible underlying basis of the different pressure-dependent tension behavior in relaxed, rigor, and active muscle is discussed.

Animals↗

PubMed1974

The interaction of the calcium-binding protein (troponin C) with bivalent cations and the inhibitory protein (troponin I).

1. The molecular weight of the calcium-binding protein of rabbit white skeletal muscle was estimated to be 18500 by sedimentation equilibrium and electrophoresis in sodium dodecyl sulphate. 2. Addition of 2 Ca(2+) ions per molecule produced reversible changes in the u.v.-absorption spectrum that are interpreted as arising from conformational changes in the structure of the protein. 3. Cd(2+) was almost as effective as Ca(2+) in producing the spectral changes. Other bivalent metal ions, particularly Mg(2+), were less effective. 4. Binding of Ca(2+) by the calcium-binding protein produced an increase in mobility to the anode on electrophoresis in 6m-urea at pH8.6. The Ca(2+)-saturated form of the protein was more retarded on gel filtration than the Ca(2+)-free form. 5. In the presence of Ca(2+) the calcium-binding protein formed an equimolar complex with the inhibitory protein. This complex was stable in 8m-urea and in the pH range 7.0-8.6. 6. An isotope-dilution method for the measurement of the content of calcium-binding protein in whole muscle is described. In rabbit psoas muscle the ratio of actin monomers to molecules of calcium-binding protein was approx. 7:1. Similar values were obtained for red skeletal and cardiac muscle. 7. Evidence is presented indicating that in the rabbit the inhibitory protein of the troponin complex of red skeletal and cardiac muscles is different from the inhibitory protein of white skeletal muscle.

Actins↗

PubMed1975

The solubility of halothane in canine blood and tissues.

In vitro measurements were made of the solubility of halothane (about 1%, carried in 5% carbon dioxide in air) in tissues taken from dogs, mostly Alsatians, and usually after about 8 hr anaesthesia with pentobarbitone and halothane. The mean Ostwald solubility coefficient lambda in atm- minus 1 at 37 degrees C, for seven to 21 animals, were: brain 6.03, gut 4.23, cardiac muscle 4.88, kidney 4.95, liver 6.64, skeletal muscle (psoas) 5.45. For the gracilis muscle solubilities up to 20 atm- minus 1 were obtained. Solubility in blood was shown to increase significantly with haematocrit and haemoglobin and to be significantly higher in blood from unanaesthetized than from anaesthetized animals. The best-estimate equations were lambda-2.38 + 0.042H for the unanaesthetized condition and lambda-1.69+0.049 H for the anaesthetized condition, where H is haematocrit %. Combining the present results with those for other species showed that the solubility of halothane increased fairly systematically from blood to kidney to brain to liver, and from ox to man to dog to rabbit.

Anesthesia↗