Evolution from Ferromagnetism to Antiferromagnetism in Yb(Rh_{1-x}Co_{x})_{2}Si_{2}.

Yb(Rh_{1-x}Co_{x})_{2}Si_{2} is a model system to address two challenging problems in the field of strongly correlated electron systems. The first is the intriguing competition between ferromagnetic (FM) and antiferromagnetic (AFM) order when approaching a magnetic quantum critical point (QCP). The second is the occurrence of magnetic order along a very hard crystalline electric field (CEF) direction, i.e., along the one with the smallest available magnetic moment. Here, we present a detailed study of the evolution of the magnetic order in this system from a FM state with moments along the very hard c direction at x=0.27 towards the yet unknown magnetic state at x=0. We first observe a transition towards an AFM canted state with decreasing x and then to a pure AFM state. This confirms that the QCP in YbRh_{2}Si_{2} is AFM, but the phase diagram is very similar to those observed in some inherently FM systems like NbFe_{2} and CeRuPO, which suggests that the basic underlying instability might be FM. Despite the huge CEF anisotropy the ordered moment retains a component along the c axis also in the AFM state. The huge CEF anisotropy in Yb(Rh_{1-x}Co_{x})_{2}Si_{2} excludes that this hard-axis ordering originates from a competing exchange anisotropy as often proposed for other heavy-fermion systems. Instead, it points to an order-by-disorder based mechanism.

Thermodynamic evidence for valley-dependent density of states in bulk bismuth.

Electron-like carriers in bismuth are described by the Dirac Hamiltonian, with a band mass becoming a thousandth of the bare electron mass along one crystalline axis. The existence of three anisotropic valleys offers electrons an additional degree of freedom, a subject of recent attention. Here, we map the Landau spectrum by angle-resolved magnetostriction, and quantify the carrier number in each valley: while the electron valleys keep identical spectra, they substantially differ in their density of states at the Fermi level. Thus, the electron fluid does not keep the rotational symmetry of the lattice at low temperature and high magnetic field, even in the absence of internal strain. This effect, reminiscent of the Coulomb pseudogap in localized electronic states, affects only electrons in the immediate vicinity of the Fermi level. It presents the most striking departure from the non-interacting picture of electrons in bulk bismuth.

Role of hyperfine coupling in magnetic and quadrupolar ordering of Pr3Pd20Si6.

We study the ternary clathrate Pr3Pd20Si6 in specific heat and ac susceptibility measurements on a high-quality single crystal, distinguishing antiferromagnetic and antiferroquadrupolar ordering, as well as a hitherto unknown magnetic low-temperature transition. The specific heat shows the direct involvement of nuclear spin degrees of freedom in the antiferromagnetic ordering, which is well supported by our calculation of the hyperfine level scheme without adjustable parameters. Pr3Pd20Si6 is, therefore, one of the rare materials where the nuclear moments are involved in the formation of the magnetic ground state.

Doped YbRh2Si2: not only ferromagnetic correlations but ferromagnetic order.

YbRh2Si2 is a prototypical system for studying unconventional antiferromagnetic quantum criticality. However, ferromagnetic correlations are present which can be enhanced via isoelectronic cobalt substitution for rhodium in Yb(Rh(1-x)Co(x))2Si2. So far, the magnetic order with increasing x was believed to remain antiferromagnetic. Here, we present the discovery of ferromagnetism for x = 0.27 below T(C) = 1.30 K in single crystalline samples. Unexpectedly, ordering occurs along the c axis, the hard crystalline electric field direction, where the g factor is an order of magnitude smaller than in the basal plane. Although the spontaneous magnetization is only 0.1 µB/Yb it corresponds to the full expected saturation moment along c taking into account partial Kondo screening.

Amino acid sequence of myoglobin from emu (Dromaius novaehollandiae) skeletal muscle.

The objective of the present study was to characterize the primary structure of emu myoglobin (Mb). Emu Mb was isolated from Iliofibularis muscle employing gel-filtration chromatography. Matrix Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry was employed to determine the exact molecular mass of emu Mb in comparison with horse Mb, and Edman degradation was utilized to characterize the amino acid sequence. The molecular mass of emu Mb was 17,380 Da and was close to those reported for ratite and poultry myoglobins. Similar to myoglobins from meat-producing livestock and birds, emu Mb has 153 amino acids. Emu Mb contains 9 histidines. Proximal and distal histidines, responsible for coordinating oxygen-binding property of Mb, are conserved in emu. Emu Mb shared more than 90% homology with ratite and chicken myoglobins, whereas it demonstrated only less than 70% sequence similarity with ruminant myoglobins.

Characterization of bison (Bison bison) myoglobin.

Bison is an alternate meat species gaining increased popularity in North America. Although previous investigations reported that bison meat discolors faster than beef, the molecular basis of this observation has not been investigated. Therefore, the objective of the present study was to determine the redox stability, thermostability, and primary structure of bison myoglobin (Mb), in comparison with beef Mb. Purified bison and beef myoglobins were analyzed for autoxidation, lipid oxidation-induced oxidation, and thermostability. Matrix Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry was utilized for determining the exact molecular mass of bison Mb, whereas Edman degradation was employed to determine the amino acid sequence. Bison and beef myoglobins behaved similarly in autoxidation, lipid oxidation-induced oxidation, and thermostability. The observed molecular mass of bison and beef myoglobins was 16,949 Da, and the primary structure of bison Mb shared 100% similarity with beef and yak myoglobins. Noticeably, the amino acid sequence of bison Mb was different from other ruminant myoglobins, such as water-buffalo, sheep, goat, and red-deer. The present study is the first to report the primary structure of bison Mb. Same primary structure and similar biochemical attributes of bison and beef myoglobins suggested that the observed rapid discoloration in bison meat could not be attributed to biochemistry of bison Mb.

Primary structure of goat myoglobin.

Color stability attributes of goat meat are different from those of sheep meat, possibly due to species-specific differences in myoglobin (Mb) biochemistry. An examination of post-genomic era protein databases revealed that the primary structure of goat Mb has not been determined. Therefore, our objective was to characterize the primary structure of goat Mb. Goat Mb was isolated from cardiac muscles employing ammonium sulfate precipitation and gel-filtration chromatography, and Edman degradation was utilized to determine the amino acid sequence. Sequence analyses of intact Mb as well as tryptic- and cyanogen bromide-peptides yielded the complete primary structure of goat Mb, which shared 98.7% similarity with sheep Mb. Similar to other livestock myoglobins goat Mb has 153 residues. Comparison of the sequences of goat and sheep myoglobins revealed two amino acid substitutions - THRgoat8GLNsheep and GLYgoat52GLUsheep. Goat Mb contains 12 histidine residues. As observed in other meat-producing livestock species, distal and proximal histidines, responsible for stabilizing the heme group and coordinating oxygen-binding, are conserved in goat Mb.

ABRF-98SEQ: Evaluation of peptide sequencing at high sensitivity.

The ABRF-98SEQ sample was the 11th in a series of amino acid sequencing studies performed by the Protein Sequence Research Group of the Association of Biomolecular Resource Facilities. This study was designed to aid participants' laboratories in determining their abilities to analyze the amino acid sequence of a peptide at high sensitivity using Edman degradation, mass spectrometry (MS), or both. ABRF-98SEQ is a 17-amino acid synthetic peptide (IFDDEIEEVQALYPTER) that resembles a typical tryptic peptide. It was distributed at the 2.8-pmol level. The sample was sent dried in a microfuge tube accompanied by instructions on solubilizing the sample and by a survey form. Including tentative calls, the correct sequence was obtained by 16% of the responding participants, compared with only 6% in the 1997 study when the low-level peptide was a minor component of a mixture. This increase probably reflects the purity of ABRF-98SEQ. A secondary factor in the increase in correct calls may be the larger number of respondents this year reporting that they perform sequence analysis at the 1- to 10-pmol level. Most respondents who obtained the correct sequence used a combination of Edman sequencing and molecular weight determination by MS. Overall, the accuracy and sensitivity of peptide sequencing by Edman degradation continue to improve and are clearly aided by the use of MS for molecular weight determination. Although peptide sequencing by MS is not yet routinely practiced by the participating laboratories, results of this study indicate that MS-derived sequence data, when properly interpreted, are valuable for correcting, completing, or corroborating sequence assignments derived by Edman.

Phosphorylation of the kinase suppressor of ras by associated kinases.

The kinase suppressor of Ras (KSR) is a loss-of-function allele that suppresses the rough eye phenotype of activated Ras in Drosophila and the multivulval phenotype of activated Ras in Caenorhabditis elegans. The physiological role of mammalian KSR is not known. We examined the mechanisms regulating the phosphorylation of this putative kinase in mammalian cells. Wild-type mouse KSR and a mutated KSR protein predicted to create a kinase-dead protein are phosphorylated identically in intact cells and in the immune complex. Phosphopeptide sequencing identified 10 in vivo phosphorylation sites in KSR, all of which reside in the 539 noncatalytic amino terminal amino acids. Expression of the amino terminal portion of KSR alone demonstrated that it was phosphorylated in the intact cell and in an immune complex in a manner indistinguishable from that of intact KSR. These data demonstrate that the kinase domain of KSR is irrelevant to its phosphorylation state and suggest that the phosphorylation of KSR and its association with a distinct set of kinases may affect intracellular signaling.

Relationship of physical performance to maturation in perimenarchal girls.

The relationship of physical performance to maturation, characterized by the onset of menarche, was examined annually from 1989 to 1992 among 61 healthy, active perimenarchal girls from 10 to 14 years. Within each age group, differences in selected physical performance variables between and among three maturity groups, early, average, and late, were compared. Subjects categorized as having early or late maturation were those whose age at menarche was minus or plus, respectively, one standard deviation from the mean age at menarche 12.70 + 0.99 yr (range 10.29-14.65). Subjects demonstrated steady progression with age in breast and pubic hair development. Weight, estimated lean body weight and fat weights, and stature increased significantly with age and maturation. With the exceptions of flexibility, bent arm hang, standing vertical jump, and relative maximum oxygen uptake, the performance measures of running speed, functional strength, explosive strength, static strength, upper body power, and aerobic power improved significantly with age and maturation. Generally more mature subjects tended to perform significantly better than the less mature, but there are fewer significant performance differences between and among maturation groups within specific age groups. Therefore, whereas more mature 10- and 14-year-old females may, within the same age group, have only a very slight advantage in some physical performance abilities over their less mature age mates, more mature females aged 11, 12, and 13 years have a greater physical performance advantage. Am. J. Hum. Biol. 9:163-171, 1997. © 1997 Wiley-Liss, Inc.

Pyruvate enhances recovery of rat hearts after ischemia and reperfusion by preventing free radical generation.

Pyruvate protects myocardium from ischemic and anoxic injury, effects that have been attributed to beneficial metabolic alterations. Pyruvate also reacts with hydrogen peroxide in vitro, and pyruvate prevents free radical injury in other organs. Hearts supplied with 2 mM of pyruvate with glucose during reperfusion recovered significantly more mechanical function (81%) than those provided with 2 mM of acetate (which does not react with free radicals) and glucose (49%) or glucose alone (27%). Pyruvate significantly reduced free radical generation during reperfusion as measured with electron spin resonance using the spin-trap 5,5-dimethyl-1-pyrroline-1-oxide. In a model of direct oxidant stress, hearts were perfused with 0.28 mM of hydrogen peroxide. In this model, loss of function was almost entirely prevented by addition of 2 mM of pyruvate. From these results we conclude an important mechanism of protection when pyruvate is supplied during reperfusion is limitation of oxygen-derived free radical damage.

Increase in the number of atrial natriuretic hormone receptors in regenerating rat liver.

Forty-eight hours after partial (approximately 67%) hepatectomy the activity of the particulate guanylate cyclase was increased by 2-fold in the regenerating rat liver. This increase was not an artifact of membrane isolation procedures, and as determined by 125I-labeled Tyr-28 atrial natriuretic hormone-(1-28) ANF binding, was accompanied by a 2-fold increase in the number of ANF receptors. The Kd of the receptors in membranes of regenerating livers was not significantly different from the Kd of the receptors in livers of sham-operated rats. The linear synthetic descysteine analog of ANF, analog I, which binds only to the 66-kDa receptors, displaced approximately 40% of the specifically bound 125I-ANF in liver membranes from both hepatectomized and sham-operated (control) animals. Affinity cross-linking studies with 125I-ANF confirmed the increase in the 116-kDa ANF receptor in membranes of regenerating livers. In perfused livers derived from control and hepatectomized animals, the basal rates of cGMP production were not significantly different. However, atriopeptin II-stimulated cGMP production was twice as great in regenerating livers as compared with controls. These data demonstrate that the increase in particulate guanylate cyclase activity observed during liver regeneration is due to an increase in the 116-kDa ANF receptor-associated activity. Additionally, our data demonstrate that the regenerating rat liver may be a valuable model with which to study the role of the hepatic ANF receptor/particulate guanylate cyclase.

The effects of exchange-inert metal-nucleotide complexes on the kinetics of beef heart mitochondrial F1-ATPase.

The inhibition of beef heart mitochondrial F1 by exchange-inert metal-nucleotide complexes was examined. Mono- and bidentate Cr(NH3)4ATP were found to be mixed noncompetitive inhibitors of F1-catalyzed ATP hydrolysis (values of Ki = 0.5 and 0.1 mM; values of alpha = 0.2 and 24, respectively). Rh(H2O)nATP was also found to be a mixed noncompetitive inhibitor of F1-catalyzed ATP hydrolysis (Ki = 0.3 mM, alpha = 0.7). These compounds were used in a series of dual inhibition experiments, along with mono- and bidentate CrATP and Co(NH3)4ATP. All the exchange-inert metal-nucleotides examined were found to be mutually exclusive inhibitors of F1, indicating that they all bind to the same site(s). It is postulated that the pKa of the metal-coordinated ligands is related to the potency of inhibition by these compounds. It appears probable that the exchange-inert nucleotide complexes are binding to site(s) in addition to the catalytic site(s) of F1.

The effect of Co(III)(NH3)4ATP on the kinetics of beef heart mitochondrial ATPase.

Bidentate cobalt(III)tetraamine adenosine triphosphate [Co(NH3)4ATP] was investigated as an inhibitor of the beef heart mitochondrial F1-ATPase. The compound was found to have a mixed noncompetitive mechanism with a Ki of 0.4 mM and an alpha of 1.4 during ATP hydrolysis. Co(NH3)4ATP also noncompetitively inhibited ATP hydrolysis in the presence of bicarbonate. ITP hydrolysis was similarly affected. Co(NH3)4ATP was also used in dual inhibitor studies with adenylylimidodiphosphate (AMP-PNP) and azide; it was found to be mutually exclusive with AMP-PNP and azide. The compound also protected the F1 from modification by 4-chloro-7-nitrobenzofurazan. These results are discussed in terms of the regulation of the ATP hydrolysis reaction.