Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.86 (clotting enzyme)
 176 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The extracts having diverse immunostimulating activities were obtained as a water-phase fraction from four bacterial species representing the 4 genera (Mycobacterium, Nocardia, Gordona, and Rhodococcus) of Mycobacteriaceae by the phenol-water method, which is commonly used for extraction of endotoxic lipopolysaccharides (LPS) from gram-negative bacteria and amphipathic substances from gram-positives. These fractions, especially those of G. aurantiaca and R. terrae, showed strong stimulatory effects on murine splenocytes, macrophages of mice and guinea pigs, the immunoadjuvant activities in guinea pigs and mice, and the distinct activities inducing a tumor necrosis factor and interferons alpha/beta and gamma in primed mice. The fractions from G. aurantiaca and R. terrae exhibited potent pyrogenicity and the ability to activate the clotting enzyme cascade of the horseshoe crab (Tachypleus tridentatus). Some of these biological activities were not very different from the potency of the reference endotoxic LPS derived from Escherichia coli or Fusobacterium nucleatum. But the test fractions neither showed the activity to prepare rabbit skin to the local Shwartzman reaction, nor reacted with anti-lipid A conventional and monoclonal antibodies. Furthermore, unlike LPS, these fractions stimulated the splenocytes of C3H/HeJ mice (LPS-Nonresponder). Although the fractions showing the above biological activities have not yet been adequately purified, they contained polysaccharides, whose main constituent sugar is mannose with a smaller amount of arabinose, fatty acids consisting primarily of palmitic, stearic, and tuberculostearic acids, and small amounts of peptides and amino sugars. Since components characteristic of known immunomodulators of bacterial origin, namely endotoxins (lipid A's), cell wall peptidoglycans, lipoteichoic acids, cord factors (trehalose dimycolates), or deoxyribonucleic acids, were practically not detected in these fractions, the agent responsible for the above bioactivities is considered to be a novel substance different from the known, bacterial immunomodulators.
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PMID:Possible existence of a novel amphipathic immunostimulator in the phenol-water extracts of Mycobacteriaceae. 244 Dec 33

Lipopolysaccharide (LPS) was isolated and purified from Wolinella recta ATCC 33238 by the phenol-water procedure and RNAase treatment. The sugar components of the LPS were rhamnose, mannose, glucose, heptose, 2-keto-3-deoxyoctonate (KDO) (3-deoxy-D-manno-octulosonate) and glucosamine. The degraded polysaccharide prepared from LPS by mild acid hydrolysis was fractionated by Sephadex G-50 gel chromatography into three fractions: (1) a high-molecular-mass fraction, eluting just behind the void volume, consisting of a long chain of rhamnose (22 mols per 3 mols of heptose residue) with attached core oligosaccharide; (2) a core oligosaccharide containing heptose, glucose and KDO, substituted with a short side chain of rhamnose; (3) a low-molecular-mass fraction containing KDO and phosphate. The main fatty acids of the lipid A were C12:0, C14:0, 3-OH-C14:0 and 3-OH-C16:0. The biological activities of the LPS were similar to those of Salmonella typhimurium LPS in activation of the clotting enzyme of Limulus amoebocytes, the Schwartzman reaction and mitogenicity for murine lymphocytes, although all the biological activities of lipid A were lower than those of intact LPS.
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PMID:Chemical and biological properties of lipopolysaccharide, lipid A and degraded polysaccharide from Wolinella recta ATCC 33238. 260 May 85

During the period of 1983 to 1987 mud and water samples were collected from 12 larger lakes on the Yunnan Plateau. The actinomycetes in both sediment and water samples were investigated. Strains producing metabolites were screened by various procedures. The results are as follow: 1. The number and composition of actinomycetes in a lake were found to have relation to the physical and chemical features of the water-body. On the basis of the number and generic diversity of actinomycetes, lakes were thus divided into four groups. 2. Micromonospora occupied a notable domonance in benthic samples taken from all 12 lakes. This is a conspicuous characteristics of actinomycete flora in these lakes. 3. The population of actinomycetes in Lakes Qilu, Yilong and Datun ranges from 2991 to 3542 X 10(3)/g dry wt. of mud. 4. Strains of Actinomadura, Microtetraspora, Micropolyspora, Saccharomonospora and Saccharopolyspora were isolated. These genera were not previously reported in similar studies abroad. In addition, five species were considered to be new to science: Micromonospora phaeovirida Jiang et Xu, 1985 Saccharomonospora yunnanensis Jiang et Xu, 1985 Microtetraspora flavorosea Jiang et Xu, 1986 Actinomadura chenghaiensis Jiang et Xu, 1986 Actinomadura viridoflava Jiang et Xu, 1986 5. Studies indicate that actinomycetes possibly play an important role in the decomposition of chitin, cellulose and some toxic substances in lakes. 6. As freshwater resources, actinomycetes produce various useful metabolites such as fibrinolysine, and milk-clotting enzyme.
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PMID:[Studies on actinomycete flora and resources in the plateau lakes in Yunnan]. 280 May 41

Lipopolysaccharides (LPSs) were extracted by phenol-water from three oral strains of Selenomonas. The preparations were tested for the ability to induce a blastogenic response in cultures of spleen cells from normal and nude BALB/c mice, to activate guinea pig complement and the clotting enzyme system of Limulus polyphemus amoebocytes, and to kill Actinomycin-D treated mice. The capacity of the three LPSs was comparable to that of enterobacterial LPS.
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PMID:Biological activity of lipopolysaccharides from oral Selenomonas. 346 99

Lipopolysaccharides (LPSs) were isolated from Bacteroides gingivalis and Escherichia coli by the phenol-water and butanol-water procedures. The phenol-water-extracted LPS from B. gingivalis 381 was composed of 46% carbohydrate, 23% hexosamine, 18% fatty acid, and 5% protein. The major component sugars of this preparation were glucose, glucosamine, rhamnose, galactose, galactosamine, and mannose, and their molecular ratio was 1:0.9:0.7:0.6:0.6:0.4, respectively. Neither heptose nor 2-keto-3-deoxyoctonate was detected. The butanol-water-extracted LPS from this strain was composed of 76% glucose, 7% fatty acid, and 13% protein, and it was associated with a number of polypeptides (13 to 56 kilodaltons). The main fatty acid of both LPS preparations was palmitic acid. It was found that biological activities of LPS from B. gingivalis were comparable to those of LPS from E. coli in terms of activation of the clotting enzyme of Limulus amebocyte lysate, mitogenicity, polyclonal B cell activation, and stimulation of interleukin 1 production in BALB/c mice. Furthermore, LPS-nonresponsive C3H/HeJ spleen cells were found to yield good mitogenic responses to both phenol-water-extracted LPS and butanol-water-extracted LPS from B. gingivalis or butanol-water-extracted LPS from E. coli. On the other hand, spleen cells from LPS-responsive C3H/HeN mice responded well to all these LPS preparations.
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PMID:Biochemical and immunobiological properties of lipopolysaccharide (LPS) from Bacteroides gingivalis and comparison with LPS from Escherichia coli. 388 61

Milk-clotting enzyme from a strain of Mucor varians Pispek selected in a previous work was obtained by solid culture followed by water extraction. Moistened wheat bran (120% water on dry bases) proved to be a good medium for the production of the milk-clotting enzyme. The production may be related to growth and 4,000 U milk-clotting activity by g of wheat bran was achieved. The milk-clotting enzyme was easily extracted with water from the cultures and could be precipitated by salting out with ammonium sulfate or by mixing with ethanol, methanol or acetone. The crude enzyme is an acid protease having optimal activity at pH: 3.0. Like calf rennet, this crude enzyme from M. varians loses activity with heat treatment. The level of lipolytic activity of the crude enzyme is similar to some commercial preparations and neither an antibiotic nor an amylase activity was demonstrated in the crude extracts.
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PMID:[Production and properties of the milk-clotting enzyme]. 640 Jul 64

A concentrate of milk-clotting enzyme was produced by culture of Mucor bacilliformis on wheat bran medium moistened to 120% water on dry bases with HC1 2 N solution. The wheat bran was autoclaved, spread on trays and inoculated with 5.10(6) spore/gr of dry bran. After 10 days of culture at 21 degrees C, the enzyme produced was extracted with water and adjusted to pH 4.4. The precipitation was performed with ethanol. The precipitate was dissolved in HCl solution (pH 4.5) and it was concentrated by dialysis against polyethylene glycol 20.000. The enzyme solution had a specific activity of 1123 units/mg. and it was tested in the elaboration of cream cheese.
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PMID:[Production of a concentrate of Mucor bacilliformis acid protease]. 676 21

The 64 amino acid hirudin-like peptide HM2 (Hirudinaria manillensis) is one of the agents known to specifically block the blood-clotting enzyme thrombin, and therefore is used as a potential pharmacological tool for the treatment of arterial and venous thrombosis. This peptide and its derivatives provide a new set of probes for studies aimed at elucidating the structural basis of the inhibition of alpha-thrombin. We used 581, 699, and 492 nmr-derived constraints respectively in a protocol employing simulated annealing, followed by restrained molecular dynamics and restrained energy minimization to derive the three-dimensional structures of HM2 and its mutants the HM2 (V + G) and the HM2 (1-47). HM2 consists of a well-defined core region of two double-stranded beta-sheet and a disordered C-terminus. These features are shared by other members of the hirudin family. The same type of folding has also been observed for recombinant hirudins whose structure has been determined in solution by nmr spectroscopy and in the structure of the complex hirudin-thrombin determined by x-ray diffraction. Molecular dynamics (MD) simulation methods were applied in the study of the structural and dynamic fluctuation properties of the hirudin derivatives solvated by 1625 and 1276 water molecules with periodic boundary conditions for HM2 and HM2 (1-47), respectively. Trajectories of 100 and 50 ps for the two unconstrained systems were generated at constant temperature and pressure. Analysis of the MD simulation shows that the structure of the peptide core is fairly rigid and stable in itself while the conformation of the C-terminal tail, which is involved in the inhibitory mechanism of thrombin, fluctuates and appears as a disordered region.
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PMID:NMR solution structure of a novel hirudin variant HM2, N-terminal 1-47 and N64-->V + G mutant. 912 39

The structure of two selective inhibitors, Ac-Tyr-Ile-Arg-Ile-Pro-NH2 and Ac-(4-Amino-Phe)-(Cyclohexyl-Gly)-Arg-NH2, in the active site of the blood clotting enzyme factor Xa was determined by using transferred nuclear Overhauser effect nuclear magnetic resonance (NMR) spectroscopy. They represent a family of peptidic inhibitors obtained by the screening of a vast combinatorial library. Each structure was first calculated by using standard computational procedures (distance geometry, simulated annealing, energy minimization) and then further refined by systematic search of the conformation of the inhibitor docked in the active site and repeating the simulated annealing and energy minimization. The final structure was optimized by molecular dynamics simulations of the inhibitor-complex in water. The NMR restraints were kept throughout the refinement. The inhibitors assume a compact, very well defined conformation, embedded into the substrate binding site not in the same way as a substrate, blocking thus the catalysis. The model allows to explain the mode of action, affinity, and specificity of the peptides and to map the active site.
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PMID:Mapping the active site of factor Xa by selective inhibitors: an NMR and MD study. 951 42

Lipopolysaccharides (LPSs) were purified from Actinobacillus pleuropneumoniae serotype 2, Bordetella bronchiseptica and Haemophilus parasuis serotype 5, which were used for vaccine production in Japan, by the phenol-water procedure. In SDS-PAGE analysis, A. pleuropneumoniae LPS, as well as Escherichia coli LPS, demonstrated a typical ladder profile of a smooth-type LPS. On the other hand, B. bronchiseptica and H. parasuis LPSs lacked the ladder profiles. It was found that the biological activity of these LPSs was comparable to those of E. coli LPS in terms of activation of the clotting enzyme of Limulus amoebocyte lysate, mitogenic activity of mouse spleen cells, stimulation of TNF-alpha and nitric oxide production, but IL-6 production could hardly be observed in any LPS.
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PMID:Biological activities of lipopolysaccharides extracted from porcine vaccine strains. 1065 Oct 44


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