301 research outputs found

    Demutualization and enforcement incentives at self-regulatory financial exchanges

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    n the last few years, many of the world’s largest financial exchanges have converted from mutual, not-for-profit organizations to publicly-traded, for-profit firms. In most cases, these exchanges have substantial responsibilities with respect to enforcing various regulations that protect investors from dishonest agents. We examine how the incentives to enforce such regulations change as an exchange converts from mutual to for-profit status. In contrast to oft-stated concerns, we find that, in many circumstances, an exchange that maximizes shareholder (rather than member) income has a greater incentive to aggressively enforce these types of regulations

    Ca2+ binding to Chromaffin Vesicle Matrix Proteins

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    Recently we found that Ca2+ within chromaffin vesicles is largely bound [Bulenda, D., & Gratzl, M. (1985) Biochemistry 24, 7760-77651. In order to explore the nature of these bonds, we analyzed the binding of Ca2+ to the vesicle matrix proteins as well as to ATP, the main nucleotide present in these vesicles. The dissociation constant at pH 7 is 50 pM (number of binding sites, n = 180 nmol/mg of protein) for Ca2+-protein bonds and 15 pM (n = 0.8 pmol/pmoi) for Ca2+-ATP bonds. When the pH is decreased to more physiological values (pH 6), the number of binding sites remains the same. However, the affinity of Ca2+ for the proteins decreases much less than its affinity for ATP (dissociation constant of 90 vs. 70 pM). At pH 6 monovalent cations (30-50 mM) as well as Mg2+ (0.1-0.5 mM), which are also present within chromaffin vesicles, do not affect the number of binding sites for Ca2+ but cause a decrease in the affinity of Ca2+ for both proteins and ATP. For Ca2+ binding to ATP in the presence of 0.5 mM Mg2+ we found a dissociation constant of 340 pM and after addition of 35 mM K+ a dissociation constant of 170 pM. Ca2+ binding to the chromaffin vesicle matrix proteins in the presence of 0.5 mM Mg2+ is characterized by a Kd of 240 pM and after addition of 15 mM Na' by a Kd of 340 pM. The similar affinity of Ca2+ for protein and ATP, especially at pH 6, in media of increased ionic strength and after addition of Mg2+, points to the possibility that the intravesicular medium determines whether Ca2+ is preferentially bound to ATP or the chromaffin vesicle matrix proteins. Purified chromogranin A, after sodium dodecyl sulfate- polyacrylamide gel electrophoresis, stains with a carbocyanine dye ("Stains-all") and, following blotting onto nitrocellulose, binds to 45Ca2+. A spectrophotometric analysis of dye binding to chromaffin vesicle matrix proteins revealed a strong absorption band at 615 nm for the dye-protein complex. Since the observed spectral changes were unaffected by the presence of Ca2+ (100 pM free), the sites interacting with the dye and Ca2+ must be regarded as different

    Chromogranins, widespread in endocrine and nervous tissue, bind Ca2+

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    AbstractThe proteinaceous components of the secretory vesicle contents isolated from bovine adrenal medulla bind Ca2+ (number of binding sites, 152 ± 52 nmol Ca2+ per mg protein; dissociation constant, 54 ± 8 μM (n = 5)). SDS-polyacrylamide gel electrophoresis and 45Ca2+binding of the proteins following their separation and blotting on nitrocellulose revealed that Ca2+ binds to chromogranins. Moreover, it was shown that the chromogranins, like other known Ca2+-binding proteins, can be specifically stained with a cationic carbocyanine dye. The Ca2+-binding function of the chromogranins described here, in conjunction with recent findings concerning Ca2+ transport across chromaffin vesicle membranes and the widespread distribution of chromogranins in many different endocrine and nerve cells, points to the general importance of these proteins in the metabolism ofCa2+

    The puzzle of privately-imposed price limits: are the limits imposed by financial exchanges effective?

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    Some of the world’s largest futures exchanges impose daily limits on the price movements of individual contracts. Using data from three of the most active US commodity futures contracts, we show that these price restrictions are largely ineffective because traders are able to take similar positions using other contracts. When price limits become binding on the futures market, the associated (but unrestricted) options market becomes the price discovery market: much of the trading that would have occurred on the futures market migrates to the options market, and options prices accurately predict the (unconstrained) futures price the next day. We also show that the presence of options mitigates the effect of price limits on information revelation by documenting that futures markets reflect more accurate information on days following limit hits when the associated options were trading on the previous day. Overall, our evidence suggests that price limits in US futures markets have little effect on prices when options markets exist.Price limits, Regulatory evasion, Put-call parity, Satellite market, Price discovery

    3-(3-Chloro­prop­yl)-7,8-dimeth­oxy-2,3,4,5-tetra­hydro-1H-3-benzazepin-2-one at 125 K

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    In the title compound, C15H20ClNO3, the seven-membered ring adopts a distorted boat–sofa conformation; the methyl­ene C atoms of this ring are coplanar with the benzene ring. Both meth­oxy groups are almost coplanar with the attached benzene ring [C—C—O—C = 6.5 (2) and −13.5 (3)°]. An intra­molecular C—H⋯O hydrogen bond is observed in the mol­ecular structure. In the crystal structure, a C—H⋯π inter­action involving the benzene ring is observed

    Chromogranin A in the olfactory system of the rat

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    The olfactory bulb of the rat contains chromogranin A at a similar level as the adrenal gland or the hypophysis as revealed by immunoblots. Olfactory chromogranin A also displays the same size as chromogranin A of endocrine cells. In the hippocampus and other brain regions, we could not detect chromogranin A by immunoblotting. In contrast, chromogranin A messenger ribonucleic acid (using S1 nuclease protection assays) was observed in all brain regions examined, including the olfactory bulb. By in situ hybridization histochemistry with a complementary ribonucleic acid probe (280 nucleotides), and by immunocytochemistry, chromogranin A synthesis could be localized to cell bodies of the mitral cell layer, of the external plexiform layer and of the periglomerular region of the olfactory bulb. Immunocytochemically, chromogranin A was also detected in the central projection areas of mitral and tufted cells in the primary olfactory cortex and the anterior amygdaloid area but not in the olfactory glomeruli, where the incoming olfactory nerve fibers of the primary olfactory neurons establish synaptic contacts. Taken together the data show that chromogranin A, following biosynthesis in the perikarya of the mitral and tufted cells, is specifically transported into their axonal terminals but not into their primary dendrites. We propose that the rat olfactory system could serve as a model for the study of chromogranin A regulation and function in neurons

    Processing and Transmission of Information

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    Contains reports on four research projects.Lincoln Laboratory (Purchase Order DDL-B222)United States Department of the ArmyUnited States Department of the NavyUnited States Department of the Air Force (Contract AF19(604)-5200

    Stock Inka, Time, Migration and Forced Immobility. Sub-Saharan African Migrants in Morocco

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    Le Maroc était autrefois un pays que beaucoup de personnes en provenance d’Afrique subsaharienne traversaient en direction de l’Europe. Plus récemment, pourtant, la continuation de ce trajet a été rendue difficile, voire même impossible, à cause de l’intensification du contrôle aux frontières extérieures de l’Union européenne. L’ouvrage Time, Migration and Forced Immobility. Sub-Saharan African Migrants in Morocco, écrit par la sociologue Inka Stock, part donc d’un paradoxe : alors que les ac..

    3-(3-Chloro­prop­yl)-7,8-dimeth­oxy-1H-3-benzazepin-2(3H)-one at 125 K

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    In the title compound, C15H18ClNO3, the seven-membered ring has a mirror plane passing through the methyl­ene C atom and bis­ecting the C=C bond. It adopts a bent conformation, inter­mediate between the boat and chair forms. Both meth­oxy groups are coplanar with the attached benzene ring [C—C—O—C = −0.5 (3) and 2.2 (3)°]. In the crystal structure, inversion-related mol­ecules are linked via C—H⋯O hydrogen bonds and π–π inter­actions involving the benzene ring [centroid–centroid distance = 3.6393 (12)Å]
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