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)

1. When red cells are incubated in solutions containing p-nitrophenyl-phosphate (p-NPP), intracellular p-NPP quickly builds up reaching with a half-time of 3 min a concentration in cell water equal to one fourth the external concentration, which under the conditions used is the expected value for a divalent anion in Gibbs-Donnan equilibrium. Hence p-NPP added to the incubation media in red cells has quick access to the active centre of the membrane phosphatase which is located at the inner surface of the cell membrane.2. When p-NPP is added to the incubation media of ATP-free red cells or reconstituted ghosts, no ouabain-sensitive cation movements are detectable, suggesting that hydrolysis of p-NPP by the active transport system is unable to energize active ion translocation.3. When p-NPP concentration in the incubation media of ATP-containing cells is progressively raised, both ouabain-sensitive Na loss and ouabain-sensitive Rb uptake tend to zero along rectangular hyperbolae. For both movements inhibition is half-maximal at 77 mM external p-NPP (i.e. 19 mM internal p-NPP).4. p-NPP inhibits with equal effectiveness the Na:K and the Na:Na exchanges catalysed by the Na pump.5. The inhibitory effect of p-NPP cannot be attributed to the products of its hydrolysis, is inversely related to the intracellular ATP concentration and seems to be exerted at the inner surface of the cell membrane with an apparent affinity similar to that of the membrane phosphatase. These facts suggest that inhibition is mediated by the combination of p-NPP with the active centre of the membrane phosphatase.6. Apart from affecting the ouabain-sensitive cation movements, p-NPP increases the ouabain-resistant uptake and loss of both Na and Rb. This effect is about 4 times larger for Rb than for Na, and its kinetic analysis suggests that it is due to an increase in the passive permeability of the cell membrane.7. The increase in passive cation permeability upon addition of p-NPP cannot be attributed to the products of its hydrolysis. It seems to be due to the combination of p-NPP with a site which, like the active centre of the ouabain-resistant membrane phosphatase, faces the inner surface of the cell membrane, is unaffected by ATP and is half saturated by about 15 mM-p NPP.
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PMID:Potassium activated phosphatase from human red blood cells. The effects of p-nitrophenylphosphate on carbon fluxes. 433 52

The presence of a high-molecular weight complex with acid phosphatase activity in the cytosol of human mammary tumors is reported. This complex appeared in the cytosol after tissue homogenization in the presence of dithiotreitol, with or without Triton X-100 and at acidic or neutral pH. Upon gel electrophoresis, this fraction showed only one band of enzyme activity which did not enter the fine pore gel. Lubrol or n-butanol had no apparent effect on this complex, and 8 M urea or 2% sodium dodecyl sulfate did not disaggregate this large molecule. After purification by gel filtration, ammonium sulfate precipitation and ion-exchange chromatography an apparent molecular weight or 10(6) was measured. It hydrolyzed typical acid phosphatase substrates such as p-NPP and alpha-NP, but also ATP and PPi. Only 44% inhibition was observed with L-(+)tartrate and it was still 40% active after 1 hr incubation at 60 degrees C. Reduction in the presence of SDS yielded several polypeptide bands. It was also detected in some samples of normal mammary tissues, but not in normal human placenta or liver.
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PMID:A high-molecular weight complex with acid phosphatase activity in human breast cancer. 609 19

Some properties of inorganic pyrophosphatase (PPiase EC 3.6.1.1.) and para-nitrophenylphosphatase (p-NPPase EC 3.1.3.1) in the microsomal fraction of odontoblasts were investigated. The ratio of Mg2+:p-NPP and Mg2+:PPi for optimal enzyme activities was 1:1. A mutual substrate competition for PPiase and p-NPPase was described. In the presence of 0.1 mM EDTA, Mg2+ alone was not able to reactivate p-NPPase or PPiase. Instead, Zn2+ and Co2+ reactivated the PPiase, indicating they might act as cofactors for the enzyme. Mg2+ increased the PPiase activity, probably because Mg PP2-i was the true substrate for the enzyme. The diphosphonates ethane-1-hydroxy 1,1 diphosphonate (EHDP), methane diphosphonate (MDP) and dichloromethane diphosphonate (Cl2MDP) inhibited the PPiase activity.
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PMID:Relationship of inorganic pyrophosphatase and para-nitrophenylphosphatase activities of alkaline phosphatase in the microsomal fraction of isolated odontoblasts. 612 84

The subcortical projections to the lateral dorsal nucleus (LD) of the cat thalamus were studied with retrograde transport techniques. Deposits of horseradish peroxidase (HRP) or fluorescent tracers were placed unilaterally in LD of adult cats, using electrophoretic or pressure injection techniques. Following post-injection survival periods of 1, 2 or 3 days, HRP retrogradely labeled cells were identified in sections reacted with benzidine dihydrochloride; fluorescent labeled cells were identified by fluorescent microscopy. Injections in LD result in retrogradely labeled neurons in all nuclei of the pretectal complex, including the nucleus of the optic tract (NTO), the posterior pretectal nucleus (NPP), the anterior pretectal nucleus (NPA), the pretectal olivary nucleus (NOL), and the medial pretectal nucleus (NPM). Small electrophoretic injections of HRP were used to investigate a possible topographic organization of the pretectal projections. Results from a variety of injection sites indicate only a subtle rostral-caudal gradient. That is, small injection sites in rostral LD result in retrograde labeling of neuron somata in the rostral parts of NTO, NPA and NPP, and throughout NPM. Injections in caudal LD result in labeled cells more caudally situated in NTO, NPA, NPP, and throughout NPM. Injections in the pulvinar (Pul) also result in retrogradely labeled cells in the pretectal complex, particularly NTO, NPP, and NOL. Experiments with injections of distinguishable fluorescent tracers in LD and Pul reveal that many more cells project to Pul than to LD. These experiments also reveal that while neurons that project to LD are intermingled with neurons that project to Pul, the two projections originate from separate subpopulations of cells. These results are discussed in regard to phylogenetic comparison of pretectal projections and subcortical pathways of sensory input to the limbic system.
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PMID:Projections from the pretectal complex to the thalamic lateral dorsal nucleus of the cat. 619 3

The organization of the projection from the pretectal region to the inferior olive in the cat was studied with autoradiographic and horseradish peroxidase (HRP) methods. After injections of HRP into the olive in six cats, cells were labeled ipsilaterally in the anterior pretectal nucleus (NPA), the posterior pretectal nucleus (NPP), the nucleus of the optic tract (NOT), and the dorsal terminal nucleus of the accessory optic tract (DTN). In three experiments, tritiated amino acids were injected into those parts of the pretectal region which contained labeled cells in the HRP experiments, and the projections to the olive were plotted. Both NPA and NPP projected to the rostral half of the dorsal accessory olive, the rostromedial margin of the ventral lamella, and the lateral part of the ventrolateral outgrowth. NOT projected to the caudal half of the dorsal cap, while DTN projected to both the dorsal cap and nucleus beta. The projections are entirely ipsilateral.
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PMID:Olivary projections from the pretectal region in the cat studied with horseradish peroxidase and tritiated amino acids axonal transport. 620 13

Rat bone was extracted with KCl and Triton X-100, and a tartrate-resistant acid phosphatase activity was purified by protamine sulfate precipitation, ion-exchange chromatography (CM-cellulose), and gel filtration on Sephadex G-200 according to previously described procedures. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and silver staining demonstrated a major band with an apparent monomer molecular size of approximately 14,000 Da. The enzyme is active with p-nitrophenylphosphate (p-NPP) but exhibits a 5- to 10-fold higher affinity towards several nucleotides of which ATP and ADP are the most readily hydrolyzed substrates based on kinetic studies. Based on sensitivity towards proteolytic treatment and detergent removal, as well as pH-optimum studies, a single enzyme was found to be responsible for activity towards nucleotide phosphates as well as p-NPP. This nucleotide tri- and diphosphatase constitutes around 15% of the total acid phosphatase activity in rat bone. The activity with ATP as substrate in contrast to that with p-NPP was inhibited in a noncompetitive fashion by MgCl2, sodium metavanadate, and p-chloromercuribenzoate. Enzyme activity with p-NPP and ATP is dependent on the presence of KCl and detergent and is activated by Fe3+ and ascorbate. The reported characteristics of the enzyme suggest that it functions as a unique membrane acid ATPase.
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PMID:Purification and characterization of a vanadate-sensitive nucleotide tri- and diphosphatase with acid pH optimum from rat bone. 623 50

ATPase activity (E.C. 3.6.1.3.) has been studied by electron microscopy with the help of several cytochemical techniques on Eigenmannia virescens electrocytes. Incubation was carried out with in two different media containing paranitrophenyl phosphate (p-NPP) or adenosine triphosphate (ATP) as substrate. With p-NPP the phosphate freed is captured at alkaline pH, either by strontium chloride or by lead citrate. With ATP the phosphate freed is captured at a pH close to neutrality by the lead nitrate. NaK ATPase activity was only demonstrated with the medium containing ATP; the positive results obtained with this technique were sensitive to ouabain. The enzyme is situated both on the membrane of the posterior face which is innervated and on that of the anterior face of the electrocytes. The cytoplasm of the anterior face is occupied by a strong concentration of tubules on whose membranes the enzyme is also present. The localisation of the enzyme on the tubules can explain biochemical results which indicate that 70% of the total NaK ATPase of the electrolytes is situated at the level of the anterior face.
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PMID:The cytochemical demonstration of NaK dependent adenosine triphosphatase at electrocyte level in Eigenmannia virescens (Gymnotidae). 629 6

The organization of the projection from the pretectal region to the inferior olive in the cat was studied by means of retrograde protein tracing and experimental degeneration. Small injections of horseradish peroxidase (HRP) were made into various parts of the inferior olive from a ventral approach. The number of nerve cells in the pretectal nuclei retrogradely labelled with HRP was counted and put in relation to the site of injection. Labelled cells were only found in the posterior pretectal nucleus (NPP), the nucleus of the optic tract (NOT) and the anterior pretectal nucleus (NPA). Most labelled cells were found in NPP and NOT in cases in which the rostral or caudal levels of the principal olive were labelled by the injection. NAP labelling occurred in one case with a very rostral injection of the inferior olive. Unilateral electrolytical destruction of the pretectal region produced terminal degeneration in the ipsilateral inferior olive. The heaviest ipsilateral degeneration was found in the upper half of the principal and dorsal accessory olives, and caudally in the ventrolateral outgrowth, the dorsal cap and nucleus beta with the adjacent part of the medial accessory olive. Some functional implications of the findings are discussed.
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PMID:Olivary afferents from the pretectal nuclei in the cat. 632 Jun 90

Ten peptides related to melanocyto-stimulating hormone (MSH) have been identified in an acid acetone extract of the chum salmon pituitary. All these peptides are related to the alpha-MSH and beta-MSH families, but no peptide related to gamma-MSH has been found. This result is in accordance with the finding that the gamma-MSH segment is deleted from the N-terminal peptide of salmon pro-opiocortin (NPP I). Based on the structures of newly isolated peptides, the maturation process of MSH is discussed. The major components of salmon MSH were tested for biological activities. In the lipolytic assay with rabbit fat cells, alpha-MSH I and alpha-MSH II were equipotent, but beta-MSH I and NPP I exhibited very low or no activity. On the other hand, the des-acetyl-alpha-MSH I was found to be four times as potent as alpha-MSH I in this assay. The steroidogenic activities of alpha-MSH I and N-des-acetyl-alpha-MSH I were approximately 0.05% of the potency of ovine ACTH. All other peptides exhibited less than 0.01% potency. Salmon alpha-MSHs were found to be somewhat more potent melanophore-stimulating agents than the beta-MSHs.
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PMID:Chemical and biological characterization of salmon melanocyte-stimulating hormones. 632 92

Vanadate in redox state +5 inhibited the Na+K+-activated ATPase as well as the potassium-stimulated p-nitrophenylphosphatase (p-NPPase) activities of plasma membrane fragments prepared from rat brain. Vanadate exhibited a mixed type inhibition on the Na+K+-ATP-ase activity. The same type of inhibition was observed when the p-NPPase activity of the enzyme preparation was measured either in the presence of 20 mM K+ or with 5 mM Na+ + 1 mM K+. When the reaction mixture contained 50 microM ATP, 5 mM Na+ and 1 mM K+, inhibition of p-NPP hydrolised by vanadate displayed a noncompetitive character. Higher noradrenalin concentration was required for counteracting, the inhibition of p-NPPase by vanadate in the presence of ATP than in its absence.
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PMID:Vanadate inhibition of Na+K+. ATPase and K+-dependent p-nitrophenylphosphatase: a kinetic analysis. 633 Oct 47


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