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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An improved procedure of purification of serinesulfhydrase from chicken liver is described. Preparations of enzyme (700-fold purification with the yield of 40 per cent from total activity) have been obtained homogeneous on polyacrylamide gel electrophoresis. Molecular weight of serinesulfhydrase is 90.000; 1 mole of enzyme contains 2 moles of pyridoxalphosphate and consists apparently of 2 subunits. Amino acid composition of the enzyme is studied. Absorption spectrum of serinesulfhydrase has a maximum at 430 nm what is characteristic of numerous pyridoxal-P enzymes. The position of this maximum does not depend on pH (within its range 6--10) and the presence of L-serine, a primary enzyme substrate. An essential change in the absorption spectrum of enzyme was observed in the presence of some thiol compound--DL-homocysteine, beta-mercaptoethanol and glutathione (cosubstrates of the reaction) and L-cysteine (a primary reaction substrate). It is suggested that this change in the spectrum is due to the action of SH-compounds on the enzyme conformation before the beginning of the enzymatic reaction or on its initial stages.
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PMID:[Some physical and chemical properties of serinesulfhydrase from chicken liver]. 0 Nov 9

The membrane penicillinase of Bacillus licheniformis 749/C has been demonstrated to be a phospholipoprotein. The homogeneous enzyme gives a positive reaction for phosphorous and for unsaturated fatty acids, has a molecular weight of 33,000 in contrast to 29,000 for the exoenzyme, and contains 8 to 9 additional residues of aspartate or asparagine, 4 to 5 of serine, 7 of glutamate or glutamine, and 4 to 5 of glycine per mole. The COOH-terminal sequence of both membrane and exoenzymes is -Met-Asn-Gln-Lys-COOH; hence the extra peptide portion present in the membrane enzyme is not attached to the COOH-terminus of the exoenzyme. Procedures which readily detected the lysine residue at the NH2 terminus of the exoenzyme did not yield a positive test with the membrane form. The NH2 terminus of the membrane enzyme may be blocked by or linked to the phospholipid. A procedure for the preparation of membrane penicillinase on a large scale and an improved method for purification of the exoenzyme have been developed.
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PMID:Purification of plasma membrane penicillinase from Bacillus licheniformis 749/C and comparison with exoenzyme. 0 71

The effect of benzoate anion on intramolecular general base-catalyzed ester hydrolysis by the imidazolyl group in endo-5-[4'(5')-imidazolyl]bicyclo[2.2.1]hept-endo-2-yl trans-cinnamate was examined in dioxane/H(2)O solutions. Benzoate anion exhibited a remarkable acceleration of the intramolecular general base-catalyzed hydrolysis of endo-5-[4'(5')-imidazolyl]bicyclo[2.2.1]hept-endo-2-yl trans-cinnamate by the imidazolyl group. The rate of hydrolysis in the presence of the benzoate anion increased with the dioxane mole fraction and was proportional to the concentration of benzoate anion. On the other hand, the rate of hydrolysis of endo-5-[4'(5')-imidazolyl]bicyclo[2.2.1]hept-endo-2-yl trans-cinnamate in the absence of benzoate anion decreased with the dioxane mole fraction. Thus, the ratio of the rate in the presence of benzoate anion to that in the absence of benzoate anion drastically increased with the dioxane mole fraction and attained a 2500-fold rate acceleration at a dioxane mole fraction of 0.42 (the highest experimentally attainable) when the concentration of benzoate anion was 0.5 M. The proposed mechanism involves proton abstraction by the benzoate anion from the imidazolyl group, followed by proton abstraction by the imidazolyl group from H(2)O, resulting in effective general base-catalysis of hydrolysis. The results of the present paper provide support for the "charge-relay" system in serine proteases.
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PMID:Model for "charge-relay": acceleration by carboxylate anion in intramolecular general base-catalyzed ester hydrolysis by the imidazolyl group. 1 38

1. Histamine secretion from rat peritoneal mast cells occurs spontaneously in the absence of an external stimulus. Spontaneous secretion increases as the concentration of Sr in the extracellular medium is raised from 1 to 10 m-mole/l. Ca 0.1-10 m-mole/l. does not increase spontaneous secretion.2. Spontaneous histamine secretion in the presence of Sr occurs slowly compared with evoked histamine secretion, reaching a maximum only after more than 120 min incubation with Sr 10 m-mole/l. at 37 degrees C and pH 7.6. Phosphatidyl serine, 10 mug/ml., increases the rate of spontaneous secretion in the presence of Sr.3. The spontaneous secretion occurring in the presence of Sr is highly dependent on the extracellular H ion concentration. Maximal secretion occurs at pH 8.4 and only a very limited secretion is detected at pH below 7.6. The rate of spontaneous secretion is also greater at higher pH. Inhibition of secretion caused by lowering the pH can be reversed by raising the Sr ion concentration over a limited range.4. Intact glycolytic and oxidative metabolism is required for the spontaneous secretion of histamine in the presence of Sr. Removal of extracellular glucose inhibits the secretion by about 80%, and the further addition of inhibitors of oxidative phosphorylation almost abolishes the secretion.5. Ca, Mg and Mn all inhibit the spontaneous secretion of histamine which occurs in the presence of Sr. The antagonism of the effect of Sr by Mg appears not to be competitive.6. Dibutyryl cyclic AMP, 10 mumole/l. to 3 m-mole/l. and theophylline, 30 mumole/l. inhibit spontaneous secretion in the presence of Sr. Cyclic AMP, AMP, and cyclic GMP 10 m-mole/l. are without effect on the spontaneous secretion. The inhibitory effect of dibutyryl cyclic AMP and of theophylline are dependent on pH: greater inhibition being achieved at lower pH.
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PMID:Spontaneous histamine secretion from mast cells in the presence of strontium. 7 47

The surface properties of mixed monomolecular films of retinal and phospholipids (p. lipids) are measured as a function of mole fraction at a nitrogen-water interface. An acid pH of 6.0 is maintained in the aqueous phase. Before irradiation the surface potential deltaV for 9-cis retinal, 11-cis retinal, phosphatidyl serine (PS) and phosphatidyl ethanolamine (PE), at pi=12 dyn/cm, are 490 mV, 645 mV, respectively. Before irradiation, A0 for 9-cis and 11-cis are 58 A2 and 48 A2, respectively. Experimentally measured isotherms are compared with theoretically calculated isotherms. In case of mixed films of retinal and PS the experimental isotherms are greater than theoretical, while mixed films of retinal and PE are smaller than theoretical. A maximum value for the difference between theoretical and experimental areas are obtained at (retinal)/(p. lipid)=0.1. Retinal and p. lipid do not appear to form a Schiff base, charge transfer or any other type of complex at pH 6. A eutectic type mixture between retinal and p. lipid may occur on the surface. A light induced change in deltaV of -130 mV is observed in the case of 11-cis and PE. The significance of these findings with respect to visual excitation is considered.
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PMID:Interactions between retinal and phospholipids in monomolecular films at acid pH. 12 90

A polypeptide with a molecular weight of 8 500 (HP 8 500) was isolated from the mitochondrial membrane of the nuclear mutant cni-1 of Neurospora crassa. This mutant is characterized by a cyanide-insensitive respiration and by a deficiency in the cytochromes aa3 and b. The polypeptide is synthesized on mitochondrial ribosomes. It has an extremely hydrophobic character; it is insoluble in aqueous media in the absence of sodium dodecylsulfate and is soluble in acid chloroform/methanol. It lacks histidine. The polar amino acids lysine, arginine, aspartic acid, glutamic acid, serine and threonine make up only 25% of the total amino acids on a mole-percent basis. The N-terminal amino acid is tyrosine. The possible function of this polypeptide in the mitochondrial membrane is discussed.
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PMID:Isolation and characterization of a mitochondrially synthesized polypeptide from Neurospora crassa cni-1 mutant. 12 27

Heat-denatured chicken egg white lysozyme and the reduced carboxymethylated maleylated derivative of this protein were found to serve as substrates for rabbit skeletal muscle cyclic AMP-dependent protein kinase. The native form of the protein was not a substrate. Two phosphoryl groups per mole of lysozyme were incorporated in the reaction. It was determined that the phosphoryl moieties were bound to serine 24 and serine 50 in the modified protein. Serine 24 was phosphorylated approximately 3 times as fast as serine 50. Reduced carboxymethylated maleylated derivatives of bovine serum albumin, phosphorylase b, and creatine kinase also served as substrates for the protein kinase whereas their native forms did not. The reduced carboxymethylated maleylated derivative of the inhibitory subunit of troponin was a poorer substrate than the native form of the protein. Maleylated histones F1 and F2b were also poorer substrates than the nonderivatized forms. The significance of these experiments with reference to the specificity of cyclic AMP-dependent protein kinase is discussed.
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PMID:Effect of denaturation on the susceptibility of proteins to enzymic phosphorylation. 16 38

RNA extracted from purified encephalomyocarditis (EMC) virus (EMC-RNA) can be aminoacylated with synthetase praparations from Escherichia coli, beef and rabbit liver. The extent of aminoacylation is between 0-024 and 0-080 moles per mole EMC-RNA and occurs only with serine. Either removal of possible low mol. wt. contaminants with 3 M-sodium acetate nor periodate oxidation of the virus RNA affects its aminoacylation capacity.
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PMID:Aminoacylation of encephalomyocarditis virus RNA. 18 78

The structure of bacillomycin L, an antifungal agent isolated from the culture medium of a strain of Bacillus subtilis, has been investigated. The peptide moiety contains one mole each of D-aspartic acid, L-aspartic acid, L-glutamine, L-serine, D-serine, L-threonine, and D-tyrosine. The lipid moiety is a mixture of 3-amino-12-methyltridecanoic acid (46%), 3-amino-12-methyltetradecanoic acid (38%, 3-amino-14-methylpentadecanoic acid (11%), and two minor homologues. The peptide sequence and the cyclic structure were determined by structural analysis of the peptides obtained by mild acid hydrolysis. The molecular weight was determined by the thermoosmotic method; this showed that bacillomycin L has a monomeric structure which is given in Formula 1.
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PMID:[The structure of bacillomycin L, an antibiotic from Bacillus subtilis (author's transl)]. 40 2

1. The influx of [3H]gamma-aminobutyric acid ([3H]GABA) into isolated rat superior cervical ganglia has been measured by radioassay, supplemented by autoradiography. Ganglia were incubated in oxygenated Krebs solution at 25 degrees C, containing 10 microM-amino-oxyacetic acid. Under these conditions more than 95% of accumulated tritium was unmetabolized [3H]GABA. 2. Ganglionic radioactivity increased linearly with incubation time, to yield an intracellular fluid/extracellular fluid concentration ratio (Ci/Co) of about 200 after 6 hr in 0.5 microM-external [3H]GABA. 3. Uptake showed saturation with an apparent transport constant (KT) of 6.8 microM and maximum influx velocity (Jmaxi) of 7 mumole 1. cell fluid-1- min-1. 4. The influx rate at Co = 0.5 microM was unaltered by raising intracellular GABA from 0.2 to 1 mM. 5. Influx velocity increased with temperature (5--35 degrees C) in a monotonic manner with an apparent activation energy of 14 kcal mole-1. 6. Concentrative uptake was depressed by reducing external [Na+] with ouabain, by raising [K+]o above 20 mM, or by removing external Cl-. Uptake was not particularly sensitive to Ca2+ or Mg2+ ions. 7. Utake of [3H]GABA (0.5 microM) was inhibited by beta-guanidinopropionic acid (apparent KI, 28 microM), beta-alanine (KI, 55 microM), gamma-amino-beta-hydroxybutyric acid (KI, 220 microM), beta-amino-n-butyric acid (KI, 708 microM), 3-aminopropanesulphonic acid (KI, 832 microM) and taurine (KI greater than 1 mM). Uptake was not depressed by 1 mM-glycine, alpha-alanine, leucine, serine, methionine or alpha-amino-iso-butyric acid. 8. Radioactively labelled methionine, leucine, glycine, serine, beta-alanine and taurine (concentrations less than or equal to 5 microM) were also taken up by ganglia. Of these, only uptake of beta-alanine and taurine were significantly depressed by 1 mM-GABA. 9. Autoradiographs confirmed that [3H]GABA and [3H] beta-alanine were taken up predominantly into extraneuronal sites (presumed to be neuroglial cells). Methionine, leucine, glycine and serine showed preferential accumulation in neurones. Neuronal uptake of leucine was not prevented by inhibiting protein synthesis. 10. Calculations of net fluxes from unidirectional tracer fluxes suggest that the sympathetic glial cells are capable of promoting net uptake of GABA at external concentrations above 1 microM.
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PMID:[3H]gamma-Aminobutyric acid uptake into neuroglial cells of rat superior cervical sympathetic ganglia. 50 28


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