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Biomedical subjects

Y Yeh

Publications and source records attributed to Y Yeh.

At least 73 records · Page 4Linked to original sources
PubMed1980

Antifreeze glycoproteins from Polar fish. Effects of freezing conditions on cooperative function.

Antifreeze glycoproteins and glycopeptides that function noncolligatively contribute one-third of the freezing temperature depression in the blood serum of some polar fishes and enable them to survive at low temperature (-1.9 degree C). There are at least eight closely related glycoproteins and glycopeptides ranging in molecular weight from 32,000 to 2,600 and numbered 1 to 8 in order of decreasing size. Under conditions of negligible supercooling, the glycopeptides have weaker antifreeze activity than the glycoproteins (20% on a weight basis, or 5% on a molar basis); in mixtures of both, their activities are additive. When nucleation is initiated in supercooled solutions (-4 to -5 degrees C), the glycopeptides are inactive, while the glycoproteins still show activity; when mixtures of both are nucleated in supercooled solutions, cooperative potentiation occurs, and the full activities of the glycopeptides are found. On nucleation of supercooled solutions of the glycoprotein alone or of the mixtures, the temperature rises above the freezing temperature ("overshoots") to an extent dependent upon the extent of supercooling; the temperature of the sample then decreases to form a plateau at the true freezing temperature.

Animals↗
PubMed1980

Theory of light diffraction by single skeletal muscle fibers.

A theoretical discussion is presented describing the diffraction of laser light by a single fiber of striated muscle. The complete three-dimensional geometry of the fiber has been taken into consideration. The basic repeated unit is taken as the sarcomere of a single myofibril, including its cylindrical geometry. The single fiber is considered as the sum of myofibrils up to the fiber dimensions. When proper phasing is taken into account, three cases of interest are analyzed. (a) When the adjacent myofibrils are totally aligned with respect to their index of refraction regions (e.g., A and I bands), then the diffraction pattern reflects that of a larger striated cylinder with the dimensions of the fiber. (b) When a particular skew plane develops for the myofibril elements, additional Bragg reflection occurs at certain specific sarcomere lengths, and intensity asymmetry amongst the diffracted orders occurs. (c) When the myofibril phasing changes in a random fashion, while all sarcomeres remain at the same length, then intensity decrease is directly related to the phase deviation from a reference phase point. This condition may well describe a fiber undergoing active isometric contraction.

Chemical Phenomena↗
PubMed1979

Conformations of denatured and renatured ovotransferrin.

Conformational properties of native, denatured, and renatured ovotransferrin were studied. The samples were denatured either in 7.2 M urea or in acidic (pH 3.0) conditions for periods up to a few hours. Combined data from quasielastic light scattering and transient electric birefringence were used to estimate the molecular dimensions under the various conditions. The native ovotransferrin is best described as a prolate ellipsoid with a major axis a = 68 A and a minor axis b = 21 A. Such an ellipsoidal shape is consistent with a globular particle where the solvation factor is approximately 0.28 mg/mg of solute. The urea-denatured sample was more expanded and more globular than the native sample. This observation was supported by a decrease in helical content, which was shown using circular dichroism data. Complete recovery of conformation and capacity to form a colored complex with Fe3+ seemed to occur with the simple dilution of urea or by adjustment of the low pH sample to pH 7.3.

Circular Dichroism↗
PubMed1979

Light diffraction study of single skeletal muscle fibres.

Light diffraction patterns from isolated frog semitendinosus muscle fibers were examined. When transilluminated by laser light, the muscle striations produce a diffraction pattern consisting of a series of lines that are projected as points onto an optical detector by a lens system. Diffraction data may be sequentially stored every 18 ms for later processing by digital computer systems. First- and second-order diffraction line intensities were examined from intact, chemically skinned, and glycerinated single fibers. The diffraction line intensities demonstrated a strong length dependence upon passive stretch from reference length to 3.6 micrometer. The first-order intensity linearly increased an average of 15-fold over the range examined. The magnitude of the second order intensity was less than the first order and showed an exponential rise with increasing length. Both first- and second-order intensities decreased upon muscle activation. Data from chemically skinned and glycerinated single fibers were not significantly different from intact fibers, indicating that the membrane structure has little effect upon the diffraction phenomenon in muscle. Theoretical model systems are examined in an attempt to find the basis of these results. Neither an analysis based on a diffraction grating with variable spacing nor the unit cell model of Fujime provides an explanation for the observed length dependency of intensity. Though the origin of the intensity decrease upon stimulation is not known, we have suggested that it could result from lateral misalignment of myofibrils and can occur upon activation.

Animals↗
PubMed1978

Cooperative functioning between antifreeze glycoproteins.

Antifreeze glycoproteins from polar fish bloods are a mixture of closely related components which differ structurally by size and by the presence of proline in the smaller components. Although the smaller components containing proline exist in higher amounts than do the larger ones, their presence puzzled investigators because they had very weak antifreeze activity. A very important function for these smaller components has now been found. These smaller antifreeze glycoproteins (10 to 25 mg/ml) have now been tested as mixtures with the larger active antifreeze glycoproteins (2 to 4 mg/ml) and a very large (2- to 8-fold) potentiation of antifreeze activity has been observed. There appears to be a cooperative functioning between the larger and smaller components.

Animals↗
PubMed1978

Dynamic light scattering characterization of the detergent-free, delipidated (Ca2+ + Mg2+)-ATPase from sarcoplasmic reticulum.

Dynamic light scattering studies have been conducted on the delipidated and detergent-removed (Ca2+ + Mg2+)-ATPase protein assemblies. Specific characterization of the state of aggregation and the extent of conformation change upon delipidation and detergent removal has been made. The results show that the prominent species are dimers and tetramers of very globular nature, with axial ratios of less than 2 : 1. The hydrodynamic radii of the dimers and the tetramers are, respectively, 57.5 A and 74.5 A. The globular nature of these observed entities differ from the delipidated ATPase proteins recently obtained (LeMaire, M., Jorgensen, K.E., Roigaard-Petersen, H. and Moller, J.V. (1976) Biochemistry 15, 5805--5812. Present results suggest that upon the removal of detergents from the lipid-free ATPase protein assembly, only a rather limited degree of aggregation takes place. Such a condition is consistent with models of the membrane protein system which has limited regions of hydrophobic contact. Oligomeric assemblies with aqueous channels is a possible active Ca2+ transport model consistent with results of the present data, as well as the data from several other recent studies.

Adenosine Triphosphatases↗
PubMed1976

Antifreeze glycoproteins from Antarctic fish. Inactivation by borate.

Antifreeze glycoprotein, which has previously been shown to be inactive in the presence of borate, migrates electrophoretically as the borate complex, presumably through formation of borate complexes with hydroxyl groups on the sugar side chains. Antifreeze glycoprotein (5 mg/ml) has been found to be completely active in the presence of 0.1 M borate at pH 7, but inactive at pH 9. A titration curve of pH versus the antifreeze activity of glycoprotein (5 mg/ml) in 0.1 M borate showed a progressive decrease in antifreeze activity as the pH was increased. Concomitant with decreases in activity were increases in binding of borate. At pH 9.0, nearly 2 mol of borate were complexed per glycotripeptide. Ultracentrifuge analyses showed similar molecular weights and laser quasi-elastic light scattering showed similar diffusions at pH 7.0 and 9.0 in borate and in the absence of borate. The binding of borate, rather than a change in conformation, is thus directly related to the loss of antifreeze activity. Alkaline borate also decreased hemagglutinating activity of Osage orange lectin and decreased the inhibition of the activity by the antifreeze glycoproteins.

Aldehydes↗
PubMed1976

Raman spectra of a solid antifreeze glycoprotein and its liquid and frozen aqueous solutions.

Raman spectroscopy was used to study the anomalous decrease in the freezing temperature of water produced by an antifreeze glycoprotein obtained from the sera of an Antarctic fish. An active fraction of this glycoprotein has a molecular weight of approximately 18,000 by equilibrium sedimentation compared to an apparent weight of 20 by freezing temperature depression. The Raman spectra of water present in a 1% antifreeze glycoprotein solution and of ice frozen from this solution were indistinguishable from the spectra of pure water and ice, respectively. These results indicate that the bulk properties of water and ice are unaffected by the presence of the antifreeze glycoprotein. Raman measurements on ice grown slowly, using as seed an oriented single crystal of ice in contact with 1% glycoprotein solutions, showed that the active glycoprotein was not excluded from the ice phase. On the other hand, we found that a smaller, inactive glycoprotein was excluded. Comparison of the Raman spectra of active and inactive glycoprotein components as solids, in 5% solutions, and rapidly frozen 5% solutions, showed that the two components differ in conformation and possibly in the environment of their carbohydrate hydroxyls. These observations suggest that hydrogen bonding of the carbohydrate hydroxyls of the active glycoprotein at the ice-solution interface may physically prevent growth of the ice lattice.

Adaptation, Physiological↗
PubMed1976

Raman spectroscopic investigations of sarcoplasmic reticulum membranes.

Raman spectra are presented for sarcoplasmic reticulum membranes. Interpretation of the 1000-1130 cm-1 region of the spectrum indicates that the sarcoplasmic reticulum membrane may be more fluid than erythrocyte membranes that have been examined by the I portion of the membrane spectrum with a strong 1658 cm-1 band characteristic of C=C stretching in hydrocarbon side chains exhibiting cis conformation. This band is unaltered in intensity and position in H2O and in 2H2O thus obscuring amide I protein conformation. Of particular interest is the appearance of strong, resonantly enhanced bands at 1160 and 1527 cm-1 attributable to membrane-associated carotenoids.

Animals↗
PubMed1976

A light-scattering characterization of membrane vesicles.

A technique has been developed in this paper which enables quasi-elastic laser light scattering to be used to accurately and quantitatively measure the average vesicle diffusion coefficient and the relative dispersion in the diffusion coefficient about this average for dilute polydisperse vesicle suspensions. This technique relies on a theoretical analysis of a modified form of the Z-averaged diffusion coefficient. This modified Z-averaged diffusion coefficient explicitly incorporates vesicle size, structure, and polydispersity in a description of the scattered light autocorrelation spectrum. Light-scattering experiments were performed on a dilute, lobster sarcoplasmic reticulum vesicle suspension and the measured average diffusion coefficient and the diffusion coefficient relative dispersion about this average were determined with accuracies of 2 and 10%, respectively. A comparison of vesicle size inferred from light-scattering results was made with size results from electron microscopic analysis of the same sample.

Animals↗
PubMed1976

A light-scattering measurement of membrane vesicle permeability.

Light-scattering/intensity autocorrelation measurements of vesicle diffusivity were used to follow the time course of the osmotic response of lobster abdominal sarcoplasmic reticulum vesicles to five lipophobic nonelectrolytes. Steady-state portions of the resulting time traces show these vesicles to be permeable to ethylene glycol and glycerol and impermeable to erythritol, glucose, and sucrose. Using measured values of the hydrodynamic radii of these nonelectrolytes, it is concluded that under passive transport conditions, these vesicles may be thought of as having pores whose radii lie between 3.1 and 3.5 A. In addition, the results presented here indicated that above a certain impermeable nonelectrolyte concentration, vesicles did not respond osmotically even though they had not collapsed. This suggests that at least under the experimental conditions reported here, vesicles behaved as if rigid when their average volume had decreased to about 50% of its original isotonic value.

Animals↗
PubMed1975

Antifreeze glycoproteins from an Antarctic fish. Quasi-elastic light scattering studies of the hydrodynamic conformations of antifreeze glycoproteins.

A quasi-elastic light-scattering technique was used to study the hydrodynamic conformations of antifreeze glycoproteins from an Antarctic fish. Antifreeze glycoprotein is composed of repeating units of Ala-Ala-Thr, with each threonine O-linked to a disaccharide, and it exists as several polymers of different numbers of this repeating unit. Molecular weights of the two major active polymers are 10,500 and 17,500 by such methods as centrifugation and osmotic pressure, but smaller than 20 by freezing-point depression. Translational diffusion coefficients at 20 degrees were 8.35 times 10-7 cm2 s-1 and 6.15 times 10-7 cm2 s-1 for the M-r-10,500 and 17,500 polymers, respectively. Measurements at -0.2 degrees in the presence of ice crystals did not indicate any conformational changes that might be related to the lowering of the freezing temperature. Lowering the temperature of these glycoprotein solutions close to temperatures of freezing caused a decrease in the effective hydrodynamic radius of both active and inactive glycoprotein components.

Animals↗
PubMed1975

Lipid biosynthesis in the chick. A consideration of site of synthesis, influence of diet and possible regulatory mechanisms.

Studies in vitro and with intact chicks support the view that liver is the major site of lipid biosynthesis in the chicken. Adipose tissue is relatively unimportant as a site of fatty acid biosynthesis in this species although it does have the ability to esterify fatty acids to triglycerides. The available evidence, therefore, suggests that in the chicken, and presumably other avian species, fatty acids are synthesized in liver and are transported as triglycerides in the plasma low-density lipoproteins to the adipose tissue for storage. Fasting, even for short periods of time, markedly depresses the capacity for hepatic lipogenesis in the chick. Food restriction for 2 hr. depresses hepatic lipogenesis by about 90% and refeeding for 1 hr./or/the intravenous administration of glucose or fructose restores the lipogenic capacity. Feeding diets high in fat or protein cannot be adequately explained on the basis of the reduction of dietary carbohydrate which accompanies increased dietary protein or fat levels. Dietary fat and protein appear to exert their effects on hepatic lipid synthesis by different mechanisms. The depression in hepatic fatty acid synthesis brought about by fasting or fat-feeding is accompanied, and probably preceded, by an increased plasma free fatty acid level. Under these conditions hepatic fatty-acyl CoA levels increase while free CoA levels are reduced. Long-chain acyl CoA derivatives are capable of inhibiting acetyl CoA carboxylase activity as well as citrate transport. The reduced availability of free CoA may limit the citrate cleavage reaction. Dietary alterations influence the hepatic lactate-pyruvate ratio of chicks, however the changes observed are not always consistent with the changes observed in rat liver. Chicks fed high-protein diets have a decreased hepatic lactate/pyruvate ratio indicative of a more oxidized cytoplasmic environment. This change in redox state may be associated with control of fatty acid synthesis in chicks fed high-protein diets. Thyroxine and glucagon affect hepatic fatty acid synthesis in the chick, however insulin appears to play a lesser role.

Acetates↗