Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Coagulation Factor VII from bovine plasma is a glycoprotein containing a single peptide chain. The NH2-terminal sequence of Ala-Asx-Gly-Phe-Leu- is homologous with the NH2 termini of prothrombin, Factor IX, and the light chain of Factor X. Factor Xa in the presence of calcium ions and phospholipid cleaves Factor VII at an Arg-Ile bond in the sequence Arg-Ile-Val-Gly-Gly-, producing a two-chain molecule with at least 85 times the coagulant activity of single-chain Factor VII and a new NH2-terminal sequence homologous with the corresponding chains of thrombin, Factor IXa and Factor Xa. A second slower cleavage at an Arg-Gly bond destroys Factor VII activity. Bovine Factor VII, unlike prothrombin, Factor IX, and Factor X, is rapidly inhibited by diisopropylphosphorofluoridate (iPr2PF). [3H]iPr2PF is readily incorporated into one-chain, two-chain, and three-chain forms of Factor VII up to ratios of approximately 0.9 moles of [3H]diisopropylphosphate per mole of protein. The radioactive peptides generated from each form of [32P]iPr2PF-inhibited Factor VII by tryptic and thermolytic digestion were found to migrate together on paper electrophoresis. This indicates that the iPr2PF is incorporated stoichiometrically into the same specific site in each form.
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PMID:Mechanism of activation of bovine factor VII. Products of cleavage by factor Xa. 95 65

Intracellular perfusion of giant axons from Loligo forbesi with a crude protein extract of Pronase dissolved in a KF solution suppresses the process of fast inactivation of the Na conductance (the h-process in the Hodgkin-Huxley terminology). 2. The results with protease inhibitors indicate that the most substrate specific endopeptidase present in pronase, alkaline proteinase b, destroys the h-process. 3. After destruction of the inactivation the conductance rise upon depolarization followed cube law kinetics. Values of the time constant taum before and after destruction of the h-process were very similar. 4. After destruction of the inactivation process the following properties were tested: cation selectivity, instantaneous conductance and internal receptor sites for tetrodotoxin (TTX) and tetraethylammonium (TEA). No detectable changes in selectivity or instantaneous conductance were observed. No internal receptors for TTX affecting the Na conductance were found but a TEA receptor is exposed by the protein hydrolysis. 5. TEA derivatives (triethylammonium, TEA-, with an aliphatic chain, Cn) induce a partial block of the steady-state sodium current and induce a time-dependent blockage of the conductance. 6. The first effect of TEA-Cn could be described in terms of a unimolecular reaction with the following equilibrium constants: 50, 2-5, 1-0, 0-4 and 0-025 mM for TEA-C2, TEA-C4, TEA-C5, TEA-C7 and TEA-C9 respectively. 7. From the dependence of the equilibrium dissociation constant on the length of the alkyl chain we estimated the free-energy change in 560 cal/mole of CH2. The gain in free energy per CH2 group transferred from aqueous medium to the interior of a non-polar medium is 1000 cal. 8. Although with the data at hand it is impossible to propose the amino-acid sequence of the site cleaved by alkaline proteinase b, we propose that an important functional component is arginine (or lysine).
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PMID:Destruction of the sodium conductance inactivation by a specific protease in perfused nerve fibres from Loligo. 99 46

Human urinary kallikrein [EC 3.4.21.8] (HUK) was purified about 200-fold with an overall yield of 40 percent from crude powder by DEAE-cellulose chromatography, acetone fractionation, Sephadex G-100 gel filtration and DEAE-Sephadex A-50 chromatography. Its activity was 200 kallikrein units (KU) per A280. HUK from active fractions obtained by DEAE-Sephadex A-50 chromatography was separated into three active components showing isoelectric points of 3.9 (HUK-1), 4.0 (HUK-2), and 4.2 (HUK-3) by isoelectric focusing: each HUK component was homogeneous on disc electrophoresis. The approximate molecular weights of HUK-1, -2 and -3 were estimated to be 2.7 X 10(4), 2.7 X 10(4), and 2.9 X 10(4), respectively, by gel filtration on a Sephadex G-100 column. The optimum pH's of HUK-1, -2, and -3 in esterolytic action were found to be 8.0, 8.3, and 7.5, respectively, and they were fairly heat stable in comparison with other glandular kallikreins. The three components of HUK were weakly inhibited by Trasylol, but were not affected by soybean and ovomucoid trypsin inhibitors. They were strongly resistant to treatment with urea and weakly resistant to treatment with guanidine. The activation energies of HUK-1, -2, and -3 were found to by 1.17 X 10(4), 5.1 X 10(3), and 1.45 X 10(4) cal per mole, respectively. The Km values were estimated toward N-alpha-tosyl-L-arginine methyl ester (TAME), N-alpha-benozyl-L-arginine ethyl ester (BAEE), and N-alpha-benozyl-L-arginine methyl ester (BAME).
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PMID:Studies on urinary kallikreins. I. Purification and characterization of human urinary kallikreins. 108 37

A radioimmunological method for the determination of the human antidiuretic hormone [8-arginine]-vasopressin (AVP), is described in detail. The antiserum has been raised in rabbits injected with AVP adsorbed onto charcoal particles and is used at a final dilution of 1:200,000. It contains antibodies directed specifically against the C-terminal tripeptide and possesses a high association constant of 8.2 x 10(12) 1/mole. AVP is labelled in monoiodinated form (as proven after pronase digestion) at a high specific activity close to the theoretical maximum after purification from unlabelled hormone on Sephadex gel. The standard curves are characterized by a Bo of 55%, a limit of detection ascertained at least at 3 pg (10% displacement) and a 50% displacement achieved with 35.5 pg. The index of precision lambda ranges from 0.033 to 0.042. The conditions of the assay (buffer's composition and pH, timing) were systematically varied and tested. In addition the result of immunization of chicken with AVP is reported. The assay is adequate for the measurement of AVP in urine and plasma and will be described in forthcoming papers.
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PMID:Radioimmunoassay of (8-arginine)-vasopressin. I. Methodology. 124 61

The covalent modification of spinach leaf ADPglucose pyrophosphorylase leads to inactivation of both activator-stimulated and -unstimulated activity. Inactivation can be prevented if either the activator 3PGA or the inhibitor Pi are present during the modification. Pi proved to be more effective at protecting the enzyme from inactivation as it afforded 50% protection at 51 microM compared to 50% protection by 405 microM 3PGA. Partial modification of the enzyme using [14C]-phenylglyoxal leads to a decrease in both Vmax, A0.5 and a decrease in the ability of the 3PGA to stimulate the enzyme's activity. Modification increased the enzyme's susceptibility to inhibition by Pi and completely abolished the cooperative binding of Pi seen in the unmodified enzyme in the presence of 3PGA. Thus, phenylglyoxal appears to interfere, with the normal allosteric regulation of ADPglucose pyrophosphorylase from spinach leaf. Greater than 90% of the enzyme's activity is lost when 7.2 mol [14C]-phenylglyoxal are bound per mole of tetramer and this label is present in both the larger and small subunits. In addition, inactivation appears to involve two different arginine residues having different rates of modification.
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PMID:Evidence for an arginine residue at the allosteric sites of spinach leaf ADPglucose pyrophosphorylase. 132 86

The amino acid composition of flavokinase has been determined to contain five arginyl and four lysyl residues per mole. Flavokinase is inactivated by arginine-specific reagents. The substrates riboflavin and especially ATP impede inactivation, whereas neither of the products, ADP or FMN, protect. Among lysine-modifying reagents, only 2,4,6-trinitrobenzene sulfonic acid caused inactivation of the enzyme, especially under conditions for denaturation. In this case it was noted that the activity was enhanced at the early stage of the reaction but this enhancement was repressed in the presence of ATP along with the significant protection of activity. Results with modification of arginyl residues and incorporation of 14C-phenylglyoxal suggest that one such residue is involved in the substrate-binding site. The involvement of lysyl residues in catalytic function remains unclear, but seems less critical.
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PMID:Modification of arginyl and lysyl residues of flavokinase from rat small intestine. 133 80

The constituent amino acids of plusbacins A1-A4 were determined to be two moles of L-trans-3-hydroxyproline and one mole each of D-threo-beta-hydroxyaspartic acid, L-threo-beta-hydroxyaspartic acid, D-allo-threonine, D-serine, D-alanine and L-arginine. In plusbacins B1-B4, one mole of L-trans-3-hydroxyproline is replaced by L-proline. The fatty acid residue of A1 and B1 was determined to be 3-hydroxy-tetradecanoic acid, for A2 and B2 to be 3-hydroxy-isopentadecanoic acid, for A3 and B3 to be 3-hydroxy-isohexadecanoic acid, and for A4 and B4 to be 3-hydroxy-hexadecanoic acid. A lactone linkage was suggested to reside between L-threo-beta-hydroxyaspartic acid and 3-hydroxy-fatty acid residues by degradation experiments. The amino acid sequences of plusbacins A2 and B2 were confirmed by Edman degradation of their deacylated products, and supported by mass spectrometric studies. From the above, structures of all components of plusbacins were concluded.
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PMID:Structures of new peptide antibiotics, plusbacins A1-A4 and B1-B4. 150 Mar 46

A potent and structurally novel antimicrobial peptide was purified from the cytoplasmic granules of bovine neutrophils. Suspensions of Staphylococcus aureus and Escherichia coli were virtually sterilized by the peptide at a concentration of 10 micrograms/ml. The peptide was found to be comprised of 13 amino acids, 5 of which were tryptophan residues, and the carboxyl-terminal arginine was carboxamidated. The primary structure of the peptide, which we have named indolicidin, is H-Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2. The mole percent of tryptophan in indolicidin is the highest observed among known protein sequences. The multiple tryptophan residues presumably play an important role in the function of this unique antibiotic peptide.
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PMID:Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. 153 21

The production of riboflavin (vitamin B2) by Candida guilliermondii Wickerham cultivated on solar-containing medium was stimulated in the presence of corn oil (0.1 g%), arginine, phenylalanine (1 m mole/l) or CoSO4.7H2O (1000 micrograms/l). On the other hand, emulsifying agents strongly inhibited yeast growth and vitamin production. Similarly, FeSO4.7H2O and MnSO4.4H2O at 50 and 200 micrograms/l levels, respectively, also showed inhibitory effect. Among the tested purines, xanthine enhanced vitamin production.
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PMID:Physiological study on riboflavin production by hydrocarbon-utilizing Candida guilliermondii Wickerham. 160 56

1. Regulated physiological parameters are normally maintained at a constant level by regulatory mechanisms. Acute toxic effects develop whenever a pollutant causes a regulated parameter to be displaced beyond tolerated limits, and thus, regulated parameters may be convenient toxicity parameters. The present study indicates that delta mu Na+ across the adductor muscle membrane of Mytilus edulis is a regulated parameter, and that injuries develop whenever this parameter drops below -700 J/mole. 2. Regulatory physiological parameters may display quick and substantial changes when regulatory mechanisms are activated to counteract variations in the regulated parameters. Thus, regulatory parameters may be used as sensitive alarm parameters in environmental monitoring. The present results indicate that the phosphate index [(ATP x P-arginine)/(Pi)2], metabolic rate and strombine may be used as alarm parameters. 3. The combined response of all parameters may provide a pollutant-specific fingerprint in environmental monitoring.
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PMID:Physiological parameters in ecotoxicology. 167 77


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