Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01189 (beta-endorphin)
 21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

beta-Endorphin was measured by radioimmunoassay in post-mortem human brains. Samples of brain were taken from five discrete areas, both from control brains and brains of schizophrenic patients. No difference in beta-endorphin levels was found in these two groups of brains. beta-Endorphin was confirmed to be widely distributed in the brain, but there were considerable differences in the concentrations in different areas.
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PMID:Distribution of beta-endorphin in normal and schizophrenic human brains. 11 32

The study to an analyse of 726 samples of sea water, taken monthly (1977-1978) at 23 stations. At the basis of the data concerning the NPP of total coliformas, 75,5% of the samples point out a clean water for the bathing place, 11,04% = "acceptable" and 9,96% = "dirty". Considering the data about the MPP of fecal coliformas and of fecal streptocques, the sanitary state is reported in 94,23% "clean for the bathing place", 1,77% "acceptable" and 4% dirty.
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PMID:[Preliminary note on the study of seawater pollution of the Saharan coast of Tunisia]. 12 Oct 49

Plasma beta-MSH levels and sebum excretion rates (SER) were measured in thirty male and twelve female patients with acne vulgaris. The mean SER in both male and female patients was significantly increased as compared to normal control levels. Plasma beta-MSH levels were normal in male and female patients with acne and showed no correlation with the SER. The SER that occurs in acne cannot therefore be explained by an increased secretion of beta-MSH.
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PMID:Plasma beta-MSH levels in acne vulgaris. 12 5

Spectral and kinetic studies of the interaction of N-methylnicotinamide chloride and nicotinamide with the enzyme thiosulphate sulphurtransferase (thiosulphate: cyanide sulfurtransferase, EC 2.8.1.1) (also known as rhodanese) have been performed and compared with previous inhibition data obtained with N-1-(4-pyridyl)pyridinium chloride (NPP). Like NPP both N-methylnicotinamide chloride and nicotinamide are competitive inhibitors of rhodanese with respect to the substrate thiosulfate. Rhodanese binding of N-methylnicotinamide chloride gives rise to no charge transfer absorbtion band. In addition, the free energy of interaction (deltaG0) of NPP with rhodanese is approximately equal to the sum of the individual deltaG0 values of MNA and NA. These compounds are analogous to the two halves of the NPP structure. We conclude that NPP and N-methylnicotinamide chloride are not bound via a charge transfer mechanism. The major stabilizing influence appears to be an ionic interaction with an anionic enzyme site with accessory apolar stabilization. It is postulated that the ionized active site sulfhydryl group in rhodanese could provide the ionic site.
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PMID:A reexamination of the postulated charge transfer interactions at the active site of the enzyme rhodanese. 13 Sep 34

Effects of ATP, acetyl phosphate (AcP) and p-nitrophenyl phosphate (p-NPP) on the inhibition of the Na+, K+-ATPase activity were studied. ATP, AcP and p-NPP were found to facilitate the ouabain-induced inhibition of the enzyme activity only after the injection of these phosphorylyzing agents into the erythrocyte ghosts. Inside the ghosts Na+ ions enhanced the effects of the phosphorylyzing agents. K+ ions in the environment removed the stimulating effects of ATP, AcP and p-NPP on the ouabain-induced inhibition of Na+, K+-ATPase activity. It is concluded that the sites of AcP and p-NPP hydrolysis as well as the active center for ATP are localized on the inner surface of the cell membrane.
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PMID:[Study of the interaction of Na+ and K+-ATPase of erythrocytes with ouabain. Effect of acetyl phosphate and p-nitrophenyl phosphate]. 13 45

The reaction of the oxygen isotope exchange (18O-exchange) was studied in the course of the Na, K-ATPase reaction. It was shown that the intermediary and direct 18O-exchanges occurred in the system in the presence of both ATP and p-NPP. These findings are indicative of the same intermediate during the hydrolytic process in both cases. The intermediary 18O-exchange was activated by N-ethylmaleimide, hydroxylamine and 2.0--1.5 18O atoms, respectively. The detection of 18O-exchange Ouabain had no effect on the exchange. The levels of intermediary 18O-exchange during ATP and p-NPP hydrolyses were equal to 1.3--1.4 and 2.0--1.5 18O atoms, respectively. The detection of 18O-exchange reactions at the intermediary steps of both ATP and p-NPP hydrolyses implies the identity of certain stages in the destruction of these substrates by Na, K-ATPase.
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PMID:[18 O-exchange during ATP and n-nitrophenylphosphate hydrolysis by Na, K-ATPase from bovine brain]. 14 48

In normal adult rats anesthetized with urethane, intravenous injections of beta-endorphin (30--150 micrograms kg-1) induced a transient fall of blood pressure followed by a small hypertension and a prolonged hypotension. Prior administration of naloxone completely blocked these effects, whereas naloxone, given 1 hr after beta-endorphin, did not reverse the prolonged depressor phase of the opioid peptide. The effects of beta-endorphin on the arterial blood pressure were greatly reduced in animals pretreated with p-chlorophenylalanine, a specific depletor of serotonin. Moreover, in rats pretreated with potent serotonin antagonists such as cyproheptadine, mianserin, and metergoline, beta-endorphin did not produce a significant hypotension. Furthermore, the depressor effect of beta-endorphin was potentiated by fluoxetine, a specific serotonin uptake inhibitor. These observations suggest the participation of a serotonergic pathway in the action of beta-endorphin on the arterial blood pressure.
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PMID:Systemic administration of beta-endorphin: potent hypotensive effect involving a serotonergic pathway. 15 30

The same isoenzyme of nonspecific alkaline phosphatase (APase), assayed with p-nitrophenylphosphate (p-NPP), was shown be present in different calcifying tissues, bone, calcifying cartilage, odontoblasts and enamel organ. Indications were also found that the enzymatic degradation of inorganic pyrophosphate (PPi) in calcifying tissues is mediated by APase. By using specific APase inhibitors, it was shown that two enzymes capable of degrading ATP exist. These were characterized in dentinogenically active odontoblasts, and it was concluded that one is the classical APase, the other is a Ca2+ and Mg2+ activated ATPase, named Ca2+-ATPase. The two phosphatases were solubilized from odontoblasts and separated. The localization of APase and Ca2+-ATPase in odontoblasts was investigated by subcellular fractionation and EM histochemistry. Routine methods for fixation were found to almost completely inactivate the enzymes. By using a mild fixation technique that preserved 80% of the enzyme activity, the main localization for both APase and Ca2+-ATPase was found to be in the membranes of intercellular vesicles located in the cell body and odontoblasts process. No activity was found in the cell membranes. It is concluded that there are at least two enzymes able to degrade phosphate compounds at alkaline pH in hard tissue forming cells. One is the nonspecific alkaline phosphatase (APase; EC 3. 1. 3. 1), which is active against p-NPP, PPi, glycerophosphates and ATP among other substrates. The other is a more specific Ca2+-ATPase (EC 3. 6. 1. 3). There seems to be an intimate relation between these two enzymes in the tissue. The function of APase in biological calcification is still obscure. In contrast, the finding of an ATP dependent, intravesicularly directed, transmembranous Ca2+-transport in vesicles derived from the microsomal fraction of odontoblasts may explain the role of Ca2+-ATPase.
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PMID:Odontoblast alkaline phosphatases and Ca2+ transport. 15 9

An 18-month-old girl with virilization was found to have an encapsulated right adrenal carcinoma (2 x3 cm) with great variation in nuclear size, frequent mitoses, and possible blood vessel invasion. Preoperative urinary excretions of 17-ketosteroids, androsterone, etiocholanolone, dehydroepiandrosterone, testosterone, pregnanetriol, 3alpha-androstenol, and 3 beta-androstadienol were elevated; all showed a noticeable decrease postoperatively. Cortisol acetate, given preoperatively, produced a definite decrease in the urinary excretion of 17-ketosteroids and dehydroepiandrosterone; administration of corticotropin resulted in an increase in levels of urinary 17-ketosteroids, 17-hydroxycorticosteroids, and pregnanetriol. Urinary testosterone and 3beta-androstadienol may have diagnostic value since neither was suppressed by cortisol therapy. The behavior of both 3alpha-androstenol and 3beta-androstadienol in this study suggests that they are of adrenal origin.
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PMID:Studies of 16-androstenes in an infant with virilizing adrenal carcinoma. 15 37

The adenylate cyclase system present in a preparation enriched in plasma membranes derived from bovine adrenal cortex was investigated in considerable detail. This system is stimulated by adrenocorticotropic hormone (ACTH), by biologically active analogs of this hormone, and by fluoride ion. The preparation contains sodium-potassium- and magnesium-dependent ATPases that are markedly inhibited by 50 mM sodium fluoride. Incorporation of a pyruvate phosphokinase ATP generating system into the adenylate cyclase assay medium provided constant substrate levels. In the presence of the ATP generating system, the rate of cyclic AMP formation (basal, fluoride, and ACTH-activated) was proportional to enzyme concentration and was linear with time. Proportionality with respect to enzyme concentration as concerned the hormone-activated adenylate cyclase was achieved only when the ratio of hormone to enzyme protein was kept constant. The temperature optimum of the adenylate cyclase, basal or activated, was approximately 30 degrees. Michaelis-Menten kinetics were observed when the ratio of Mg2+ to ATP was approximately 6:1. Both calcium and ethylene glycol bis(beta-aminoethyl ether)-N,N'-tetraacetic acid completely inhibited the adenylate cyclase system at concentrations of 5 and 0.5 mM, respectively. GTP was inhibitory at concentrations of 10-2 M but had little effect at lower concentrations. Freezing in liquid nitrogen and storage at -60 degrees exerted little effect on the fluoride-stimulated enzyme but lowered hormone stimulated activity. Preincubation in the presence of ACTH afforded a high degree of stabilization of the enzyme system while preincubation with a biologically inactive analog afforded no protection.
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PMID:Adenylate cyclase system of bovine adrenal plasma membranes. 16 47


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