Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
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The reactions of three organic mercurial compounds, chlormerodrin, parachloromercuribenzoate (PCMB), and parachloromercuribenzenesulfonate (PCMBS) with intact red blood cells, hemolyzed red cells, hemoglobin solutions, and hemoglobin-free ghosts have been characterized. Both PCMB and PCMBS react with only 2 to 3 sulfhydryl groups per mole of hemoglobin in solution, whereas chlormerodrin reacts with 6 to 7. In hemoglobin-free ghosts, however, all three reagents react with a similar number of sulfhydryl groups, approximately 4 x 10(-17) moles per cell, or about 25 per cent of the total stromal sulfhydryl groups, which react with inorganic mercuric chloride. In the intact cell the membrane imposes a diffusion barrier; chlormerodrin and PCMB penetrate slowly, whereas PCMBS does not. Kinetic studies of chlormerodrin binding to intact cells reveal that the majority of stromal sulfhydryl groups is located inside the diffusion barrier, with only 1 to 1.5 per cent (or 1 to 1,400,000 sites per cell) located outside of this barrier. Reaction of PCMBS with intact cells is limited to this small fraction on the outer membrane surface. All three reagents are capable of inhibiting glucose transport in the red cell. With chlormerodrin and PCMBS it was demonstrated that the inhibition results from interactions with the sulfhydryl groups located on the outer surface of the membrane.
J Gen Physiol 1965 Mar
PMID:LOCALIZATION OF ERYTHROCYTE MEMBRANE SULFHYDRYL GROUPS ESSENTIAL FOR GLUCOSE TRANSPORT. 1432 78

In quiescent cat papillary muscles J(K), the rate of exchange of cellular K with K(42) in the steady state, has been measured in the presence and absence of NaCl over a wide range of temperatures. J(K) was found to be independent of the presence of external NaCl under the steady state conditions investigated. The Arrhenius plot for K exchange was linear over a range of temperatures from 2.5 to 37.5 degrees C in the absence of NaCl, and from 17.5 to 37.5 degrees C in the presence of NaCl. The corresponding apparent activation energies were, respectively, 10,200 and 8,800 calories/mole. J(K) in the absence of NaCl was not affected by 10(-5)M ouabain. These results are consistent with a passive distribution for the K of heart muscle cells. The observations suggest that a carrier-mediated forced exchange of K for Na does not occur during the steady state in mammalian heart muscle.
J Gen Physiol 1965 May
PMID:CAT HEART MUSCLE IN VITRO. VII. THE TEMPERATURE DEPENDENCE OF STEADY STATE K EXCHANGE IN PRESENCE AND ABSENCE OF NACL. 1432 98

Chloride permeation through the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel is blocked by a broad range of anions that bind tightly within the pore. Here we show that the divalent anion Pt(NO2)42- acts as an impermeant voltage-dependent blocker of the CFTR pore when added to the intracellular face of excised membrane patches. Block was of modest affinity (apparent Kd 556 microM), kinetically fast, and weakened by extracellular Cl- ions. A mutation in the pore region that alters anion selectivity, F337A, but not another mutation at the same site that has no effect on selectivity (F337Y), had a complex effect on channel block by intracellular Pt(NO2)42- ions. Relative to wild-type, block of F337A-CFTR was weakened at depolarized voltages but strengthened at hyperpolarized voltages. Current in the presence of Pt(NO2)42- increased at very negative voltages in F337A but not wild-type or F337Y, apparently due to relief of block by permeation of Pt(NO2)42- ions to the extracellular solution. This "punchthrough" was prevented by extracellular Cl- ions, reminiscent of a "lock-in" effect. Relief of block in F337A by Pt(NO2)42- permeation was only observed for blocker concentrations above 300 microM; as a result, block at very negative voltages showed an anomalous concentration dependence, with an increase in blocker concentration causing a significant weakening of block and an increase in Cl- current. We interpret this effect as reflecting concentration-dependent permeability of Pt(NO2)42- in F337A, an apparent manifestation of an anomalous mole fraction effect. We suggest that the F337A mutation allows intracellular Pt(NO2)42- to enter deeply into the CFTR pore where it interacts with multiple binding sites, and that simultaneous binding of multiple Pt(NO2)42- ions within the pore promotes their permeation to the extracellular solution.
J Gen Physiol 2003 Dec
PMID:Mutation-induced blocker permeability and multiion block of the CFTR chloride channel pore. 1461 19

Rhodopsin, the pigment of the retinal rods, can be bleached either by light or by high temperature. Earlier work had shown that when white light is used the bleaching rate does not depend on temperature, and so must be independent of the internal energy of the molecule. On the other hand thermal bleaching in the dark has a high temperature dependence from which one can calculate that the reaction has an apparent activation energy of 44 kg. cal. per mole. It has now been shown that the bleaching rate of rhodopsin becomes temperature-dependent in red light, indicating that light and heat cooperate in activating the molecule. Apparently thermal energy is needed for bleaching at long wave lengths where the quanta are not sufficiently energy-rich to bring about bleaching by themselves. The temperature dependence appears at 590 mmicro. This is the longest wave length at which bleaching by light proceeds without thermal activation, and corresponds to a quantum energy of 48.5 kg. cal. per mole. This value of the minimum energy to bleach rhodopsin by light alone is in agreement with the activation energy of thermal bleaching in the dark. At wave lengths between 590 and 750 mmicro, the longest wave length at which the bleaching rate was fast enough to study, the sum of the quantum energy and of the activation energy calculated from the temperature coefficients remains between 44 and 48.5 kg. cal. This result shows that in red light the energy deficit of the quanta can be made up by a contribution of thermal energy from the internal degrees of freedom of the rhodopsin molecule. The absorption spectrum of rhodopsin, which is not markedly temperature-dependent at shorter wave lengths, also becomes temperature-dependent in red light of wave lengths longer than about 570 to 590 mmicro. The temperature dependence of the bleaching rate is at least partly accounted for by the temperature coefficient of absorption. There is some evidence that the temperature coefficient of bleaching is somewhat greater than the temperature coefficient of absorption at wave lengths longer than 590 mmicro;. This means that the thermal energy of the molecule is a more critical factor in bleaching than in absorption. It shows that some of the molecules which absorb energy-deficient quanta of red light are unable to supply the thermal component of the activation energy needed for bleaching, so bringing about a fall in the quantum efficiency. The experiments show that there is a gradual transition between the activation of rhodopsin by light and the activation by internal energy. It is suggested that energy can move freely between the prosthetic group and the protein moiety of the molecule. In this way a part of the large amount of energy in the internal degrees of freedom of rhodopsin could become available to assist in thermal activation. Assuming that the minimum energy required for bleaching is 48.5 kg. cal., an equation familiar in the study of unimolecular reaction has been used to estimate the number of internal degrees of freedom, n, involved in supplying the thermal component of the activation energy when rhodopsin is bleached in red light. It was found that n increases from 2 at 590 mmicro to a minimum value of 15 at 750 mmicro. One wonders what value n has at 1050 mmicro, where vision still persists, and where rhodopsin molecules may supply some 16 kg. cal. of thermal energy per mole in order to make up for the energy deficit of the quanta.
J Gen Physiol 1952 Jan
PMID:The interplay o light and heat in bleaching rhodopsin. 1489 32

It has been shown by the work presented in this paper that it is possible to carry out a stepwise dephosphorylation of ovalbumin. With the aid of a prostate phosphatase that attacks only one of the two phosphorus-containing groups in the major component, A(1), of ovalbumin, a protein, A(2), containing 1 atom of phosphorus per mole has been prepared. Further dephosphorylation with an enzyme of intestinal origin gives a phosphorus-free ovalbumin, A(3). Plakalbumin has been similarly dephosphorylated to give P(2) and P(3). Significant changes in the electrophoretic mobility accompany each dephosphorylation step. This, together with the phosphorus content of the proteins and the crystal form, has been used to characterize and study the five modifications of ovalbumin thus produced.
J Gen Physiol 1952 May
PMID:Enzymatic dephosphorylation of ovalbumin and plakalbumin. 1495 15

Toluidine blue, applied to frog sperm under appropriate conditions, inactivates specifically the sperm nucleus, leaving the extranuclear parts of the cell undamaged. Thus, the dye-treated spermatozoa stimulate eggs to cleave normally, but contribute no chromosomes to the resulting embryos, which develop as typical gynogenetic haploids. The concentration of dye required to produce this inactivation varies with pH. Measurements made over the entire pH range which can be tolerated by sperm cells showed that in the lower part of the range (5 to 7) the effective dye concentration was about 5 x 10(-6)M; in the intermediate range (7 to 8.5) it was 1 x (-6) to 1 x (-7)M; and for the higher pH values (8.5 to 10.0) it was about 5 x (-8)M. Using sperm suspensions containing 1500 cells per c. mm. these concentrations of dye produced specific inactivation of the sperm nuclei within 7 to 60 minutes at 18 degrees C. Tests of the reversibility of the inactivation were made by transferring the sperm from the dye to a dilute Ringer's solution after a known degree of inactivation had been produced. Following removal of the dye the sperm cells were tested on eggs over a period of 2 hours. During this time there was no indication of a reversal of the inactivation. Microscopic observations of sperm treated with (-5)M or 5 X (-5)M dye show that the dye is taken up by the sperm nucleus, which is faintly but definitely stained. The dye appears to be uniformly distributed in the nucleus, while extranuclear structures remain unstained. Measurements of the amount of dye bound per sperm nucleus indicate that the minimal quantity required for complete inactivation is about 6.7 x (-18) mole, while the maximal amount which can be bound without injury to extranuclear structures is about 1.5 x (-16) mole. The value obtained for the minimal requirement (6.7 X (16) mole = 4 X (6) molecules) suggests that there are roughly 4 million binding sites in the nucleus which, when blocked by dye molecules, somehow prevent the sperm chromosomes from participating in the development of the egg.
J Gen Physiol 1952 May
PMID:An analysis of the inactivation of the frog sperm nucleus by toluidine blue. 1495 18

The measurement of hemolymph ecdysteroids using radioimmunoassay (RIA) indicates a biphasic increase during intermolt and premolt stages of the mole crab Emerita asiatica. The gradual rise during intermolt stage corresponds to vitellogenic activities in the ovary; whereas a distinctive premolt peak is characteristic of molting crustaceans. Injection experiments with 20-hydroxyecdysone (20E) during different molt cycle stages revealed the onset of precocious premolt changes, as determined by the epidermal retraction and setal development. Injection of 20E augmented protein synthesis in the ovary, hepatopancreas and integumentary tissues. Quantification of ecdysteroids in different developmental stages of ovary also indicated a progressive increase of ovarian ecdysteroids. Interestingly, the ovarian ecdysteroids after reaching a peak at C3 stage, start declining drastically to reach the lowest level at D(3-4) stage. This decline in the ovarian ecdysteroids is inversely related to rising hemolymph ecdysteroids during these active premolt stages. The hatching of the embryos, attached to the pleopods of the ovigerous females also occurs under a high titer of hemolymph ecdysteroids. In support, 20E injection at C3 stage crabs indicated a significant reduction in time duration of pleopodal embryonic development leading to hatching of zoea larvae. Understandably, the augmented hemolymph ecdysteroid titer helps in the synchronization of embryo hatching and the premolt changes, as occurring under the normal premolt conditions.
Gen Comp Endocrinol 2004 Sep 01
PMID:Hormonal coordination of molting and female reproduction by ecdysteroids in the mole crab Emerita asiatica (Milne Edwards). 1530 62

Endocrine cell distribution within the islets of Langerhans may vary both between species and under different energetically demanding conditions such as cold acclimation. The naked mole-rat, Heterocephalus glaber, lacking an effective insulatory pelage, is effectively a poikilotherm, yet it shows a typical mammalian cold-acclimation response by substantially increasing food intake to meet higher energy requirements when housed at lower temperatures. The endocrine component of the pancreas of thermoneutral and cold-acclimated naked mole-rats was thus characterized using immunocytochemistry and ultrastructural analyses. Four distinct endocrine cells were identified: alpha (glucagon-producing), beta (insulin-producing), delta (somatostatin-producing), and PP (pancreatic polypeptide-producing) cells. Distribution of these cells differed from that of other rodents, in that beta cells formed the mantle while alpha cells formed the core of the islets. This distribution may contribute to the observed insulin insensitivity of this species, as indicated in abnormal responses to glucose tolerance tests. Insulin-producing cells, however, were more numerous than glucagon-producing cells. This ratio was unchanged with cold acclimation. Immunoreactivity of alpha and beta cells was more intense in cold-acclimated than in thermoneutral animals, possibly indicative of a change in hormonal production in animals housed at a lower temperature.
Gen Comp Endocrinol 2004 Dec
PMID:The pancreas of the naked mole-rat (Heterocephalus glaber): an ultrastructural and immunocytochemical study of the endocrine component of thermoneutral and cold acclimated animals. 1556 Aug 67

Screening tests for glutamate producing strains were carried out, with the media containing carbohydrate and ammonia source as chief ingredients. Glutamate as well as certain other amino acids was detected by paper chromatography in culture broth of many microorganisms tested. Accumulation of L-glutamate in a significant amount (at least a few mg of glutamate per ml of broth) has been demonstrated by various strains of bacteria, streptomycetes, yeasts, and fungi. The highest level of glutamate production has been obtained by a new species of Micrococcus, yielding as much as 0.25 mole of it from one mole of glucose. The courses of fermentations mainly by known strains of microorganisms are shown. The importance of the cultural condition and strain specificity for the production of amino acids are briefly described.
J Gen Appl Microbiol 2004 Dec
PMID:Studies on the amino acid fermentation. Part 1. Production of L-glutamic acid by various microorganisms. 1596 88

TRPM7 is unique in being both an ion channel and a protein kinase. It conducts a large outward current at +100 mV but a small inward current at voltages ranging from -100 to -40 mV under physiological ionic conditions. Here we show that the small inward current of TRPM7 was dramatically enhanced by a decrease in extracellular pH, with an approximately 10-fold increase at pH 4.0 and 1-2-fold increase at pH 6.0. Several lines of evidence suggest that protons enhance TRPM7 inward currents by competing with Ca(2+) and Mg(2+) for binding sites, thereby releasing blockade of divalent cations on inward monovalent currents. First, extracellular protons significantly increased monovalent cation permeability. Second, higher proton concentrations were required to induce 50% of maximal increase in TRPM7 currents when the external Ca(2+) and Mg(2+) concentrations were increased. Third, the apparent affinity for Ca(2+) and Mg(2+) was significantly diminished at elevated external H(+) concentrations. Fourth, the anomalous-mole fraction behavior of H(+) permeation further suggests that protons compete with divalent cations for binding sites in the TRPM7 pore. Taken together, it appears that at physiological pH (7.4), Ca(2+) and Mg(2+) bind to TRPM7 and inhibit the monovalent cationic currents; whereas at high H(+) concentrations, the affinity of TRPM7 for Ca(2+) and Mg(2+) is decreased, thereby allowing monovalent cations to pass through TRPM7. Furthermore, we showed that the endogenous TRPM7-like current, which is known as Mg(2+)-inhibitable cation current (MIC) or Mg nucleotide-regulated metal ion current (MagNuM) in rat basophilic leukemia (RBL) cells was also significantly potentiated by acidic pH, suggesting that MIC/MagNuM is encoded by TRPM7. The pH sensitivity represents a novel feature of TRPM7 and implies that TRPM7 may play a role under acidic pathological conditions.
J Gen Physiol 2005 Aug
PMID:Potentiation of TRPM7 inward currents by protons. 1600 28


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