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

The production of a milk-clotting enzyme by Aspergillus versicolor in 19 different culture media was investigated. Considerable milk-clotting activity was achieved by supplying corn steep liquor with either glucose of maltose. Dephytinization of corn steep liquor had an adverse effect on the production of milk-clotting enzyme. The results indicated that complex organic compounds favoured the production of the enzyme. Precipitation with acetone or tannin was unsuitable, but ammonium sulphate and ethanol above certain concentration produced active fractions.
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PMID:Production and isolation of milk-clotting enzyme from Aspergillus versicolor. 12 98

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

A fibrinogen-clotting enzyme from the venom of the Peruvian bushmaster snake was purified to homogeneity by gel filtration on Sephadex G-100 followed by DEAE-cellulose ion-exchange chromatography using a linear ionic strength gradient with NaCl. The specific activity of the enzyme was 866 NIH U/mg, representing a 55-fold purification, with a recovery of 45%. The amino acid composition was Asx30, Thr14, Ser15, Glx33, Pro23, Gly22, Ala15, Val22, Cys18, Met3, Ile18, Leu23, Tyr2, Phe13, His8, Lys11, Arg11. The total carbohydrate content was 13.4%, comprised of 3.4% hexose, 8.7% hexosamine and 1.3% sialic acid. The enzyme was active against the synthetic amide substrate alpha-N-benzoyl-DL-arginine-p-nitroanilide (BAPNA) and against the ester substrates alpha-N-benzoyl-L-arginine ethyl ester (BAEE) and tosyl-L-arginine methyl ester (TAME). Kinetic parameters for TAME esterolysis were: Vmax, 135 mumoles/min/mg and Km, 2.5 x 10(-4) M. The pH optimum was 8.0. Vmax for BAPNA amidolysis was 0.363 mumoles/min/mg and Km, 7.5 x 10(-5) M. Enzyme activity was reduced by diethylpyrocarbonate and by photo-oxidation, suggesting that the enzyme is a serine protease with a histidine residue involved in the active site. The enzyme released fibrinopeptide A rapidly from purified human fibrinogen and fibrinopeptide B more slowly. Factor XIII was not activated and the clotting activity was not inhibited by heparin. A dose of 50 micrograms/kg brought about defibrinogenation in anaesthetized rats but rabbits were unaffected. A dose of 80 micrograms/kg defibrinogenated conscious rats after 5 hr. There were no hypotensive or haemorrhagic effects.
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PMID:Isolation and characterization of a fibrinogen-clotting enzyme from venom of the snake, Lachesis muta muta (Peruvian bushmaster). 261 37

Autoclaved aqueous extracts of Candida albicans cells (and the glucans isolated from them) give a positive reaction with a chromogenic substrate combined with amebocyte lysates of the Japanese horseshoe crab, Tachypleus tridentatus (CS-TAL). The extracts and glucans activate the lysate enzyme compound G, which in turn activates clotting enzyme. Activated clotting enzyme causes a positive CS-TAL reaction. C. albicans extracts and glucans react positively with a commercially available, unaltered CS-TAL preparation (Toxicolor), but they give a negative reaction with a CS-TAL from which compound G has been excluded (Endospecy). An autoclaved, sterile preparation of Sabouraud glucose broth used as a control in one experiment gave (like Candida extracts) a positive reaction with Toxicolor and a negative reaction with Endospecy. We found that the peptone powder used to make the Sabouraud glucose broth was contaminated with a strain of Bacillus subtilis. Autoclaved aqueous extracts of culture-grown B. subtilis cells were positive with Toxicolor and negative with Endospecy. This was also the case with two other strains of B. subtilis. Polysaccharides obtained from these extracts gave the same result. Endotoxin activates clotting enzyme through activation of the lysate enzyme compound C, which is present in both Toxicolor and Endospecy. Endotoxin, therefore, reacts with both CS-TAL preparations. Simultaneous assay with Toxicolor and Endospecy distinguishes endotoxin from fungal products, but since products of fungi and B. subtilis both give a positive Toxicolor and a negative Endospecy test, a simultaneous assay cannot differentiate them. However, this does not decrease the clinical value of the simultaneous Toxicolor-Endospecy assay for distinguishing fungal infection from endotoxemia because B. subtilis so rarely causes disease that it can be excluded from clinical consideration.
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PMID:Reaction of Bacillus subtilis products with amebocyte lysates of the Japanese horseshoe crab, Tachypleus tridentatus. 313 87

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

Chemical and biological studies were performed on lipopolysaccharide isolated from Selenomonas sputigena ATCC 33150T, a possible causative agent of periodontal diseases. The sugar components of the lipopolysaccharide of S. sputigena were mannose, galactose, glucose, L-glycero-D-mannoheptose (heptose), 2-keto-3-deoxy-octonic acid, glucosamine and galactosamine in a molar ratio of 0.3:1.0:1.0:1.0:0.2:3.0:3.2 (mol/mol heptose). Sephadex G-50 chromatography of the polysaccharide portion of the lipopolysaccharide obtained by partial hydrolysis yielded three fractions: the O-polysaccharide chain attached to the core oligosaccharide, the core oligosaccharide and monosaccharides. Compositional analysis of these fractions revealed that lipopolysaccharide of S. sputigena carries a short O-polysaccharide chain consisting of galactose and glucosamine and that the core oligosaccharide consisted of glucose, heptose, glucosamine and 2-keto-3-deoxyoctonic acid. It is of particular interest that galactosamine was detected as a component sugar of the lipid A moiety in addition to glucosamine, which is a usual component sugar of the lipid A of most gram-negative bacteria. Thus, the lipid A of S. sputigena might have a unique backbone that differs from that of the lipid A of other gram-negative bacteria. Lipid A of S. sputigena consisted mainly of fatty acids such as undecanoic, tridecanoic, tridecenoic, 3-hydroxytridecanoic and 3-hydroxytetradecanoic acid in a molar ratio of 0.4:1.0:0.3:4.0:0.5 (mol/mol tridecanoic acid). Lipopolysaccharide and lipid A from S. sputigena both exhibited biological activity in activating the clotting enzyme of Limulus amebocytes, the Schwartzman reaction, mitogenicity for murine lymphocytes and in inducing interleukin-1 alpha and interleukin-6 production in murine macrophages to the same extent as those observed for lipopolysaccharide of the Salmonella serovar typhimurium used as a positive control. The results suggested that the lipopolysaccharide of S. sputigena is a virulent factor in human periodontal diseases.
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PMID:Chemical and biological properties of lipopolysaccharide from Selenomonas sputigena ATCC 33150. 946 2

Fusarium subglutinans (Wollenweber and Reinking) Nelson et al. was found to produce intracellular milk-clotting enzyme (MCE) with good milk-clotting activity (MCA). The crude activity of the produced enzyme was recorded as optimum at 55 degrees C and pH 4.5. The highest yield i.e. 78.43 SU/mg dry biomass was obtained after 4 days of rotary shaking at 30 degrees C when the fermentation medium containes wheat flour 2%, glucose 1% and (NH4)2SO4 0.1% with an initial pH value 6.0. Under these conditions, the maximum ratio of MCA to proteolytic activity (PA) amounting to 603.31 SU/PU mg(-1) was also achieved. Production of intracellular MCE by F. subglutinans was assumed to be active growth-associated type. This enzyme preparation was less active than the calf rennet, but was superior to those of Meito's and Pfizer's rennets.
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PMID:Production of intracellular milk-clotting enzyme in submerged cultures of Fusarium subglutinans. 1172 Mar 8

Glutinous rice wine is a traditional food in south of China and it can coagulate milk. It has been proved that its function of coagulating milk is because of the presence of milk-clotting enzyme produced by microorganisms in glutinous rice wine. The aim of this work is to isolate milk-clotting enzyme producing strain from glutinous rice wine and study the fermentation condition. We screened out four bacteria and fungus by gradient dilution. It was proved that mold played the most important role in the production of milk-clotting enzyme. This is further confirmed by casein plate method. The optimization of fermentation conditions revealed that two times concentrated potato medium supplemented with 5% glucose without additional nitrogen was better for production of the enzyme. The enzyme activity was increased 144% under the conditions established.
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PMID:[Isolation and fermentation condition of milk-clotting enzyme producing strain from glutinous rice wine]. 1880 82