SEARCH · PubMed Health

Results for “Extracellular Traps”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 883 records · Page 49Linked to original sources

PubMed1997

Cloning of the TMPRSS2 gene, which encodes a novel serine protease with transmembrane, LDLRA, and SRCR domains and maps to 21q22.3.

To contribute to the development of the transcription map of human chromosome 21 (HC21), we have used exon trapping from pools of HC21-specific cosmids. Using selected trapped exons, we have identified a novel gene (named TMPRSS2) that encodes a multimeric protein with a serine protease domain. The TMPRSS2 3.8-kb mRNA is expressed strongly in small intestine and weakly in several other tissues. The full-length cDNA encodes a predicted protein of 492 amino acids that contains the following domains: (i) A serine protease domain (aa 255-492) of the S1 family that probably cleaves at Arg or Lys residues. (ii) An SRCR (scavenger receptor cysteine-rich) domain (aa 149-242) of group A (6 conserved Cys). This type of domain is involved in the binding to other cell surface or extracellular molecules. (iii) An LDLRA (LDL receptor class A) domain (aa 113-148). This type of domain forms a binding site for calcium. (iv) A predicted transmembrane domain (aa 84-106). No typical signal peptide was recognized. The gene was mapped to 21q22.3 between markers ERG and D21S56 in the same P1 as MX1. The physiological role of TMPRSS2 and its involvement in trisomy 21 phenotypes or monogenic disorders that map to HC21 are unknown.

Amino Acid Sequence↗

PubMed1986

pKa does not predict pH potentiation of sodium channel blockade by lidocaine and W6211 in guinea pig ventricular myocardium.

During diastole, tertiary amine local anesthetic molecules may exit cardiac sodium channels quickly through the membrane if they are neutral, or more slowly through the aqueous channel pore if they are charged. Extracellular acidosis potentiates sodium channel blockade by these drugs, and drug pKa should be a potent predictor of the degree of response of drug dissociation kinetics to changes in extracellular pH. To test this hypothesis, we measured kinetics of recovery from drug-induced channel blockade in guinea pig papillary muscle exposed to lidocaine (pKa 7.86) and to W6211 (pKa 6.29) using Vmax as a measure of peak sodium current. Both compounds, which are physicochemically very similar in respects other than pKa, delayed Vmax recovery in a pH-dependent fashion. As pH was lowered from 7.9 to 6.5, the recovery time constant rose from 86 to 230 msec for lidocaine and from 53 to 154 msec for W6211. We revised an earlier kinetic scheme of drug-channel interaction to incorporate newer concepts of drug trapping and ionization within the channel, and the resulting analytic expressions fit the data well. Important implications of the new scheme are that the pKa of the drug-receptor complex may differ from the drug pKa, and that deprotonation of channel-bound charged drug molecules may be a rate-limiting process.

Acidosis↗

PubMed1988

Agonist-stimulated oscillations and cycling of intracellular free calcium in individual cultured muscle cells.

Receptor regulation of [Ca2+]i was monitored in individual BC3H-1 muscle cells with intracellularly trapped fura-2 using digital imaging analysis techniques. Activation of alpha 1-adrenergic or H1-histaminergic receptors resulted in multiple bursts, or oscillations, of elevated [Ca2+]i with an average interval frequency of approximately 1.8 min-1. The duration of oscillatory behavior was generally more prolonged in response to phenylephrine than in response to histamine. Additionally, a larger fraction of the cells responded with [Ca2+]i oscillations to phenylephrine (approximately 90%) than to histamine (approximately 60%), although the majority of cells produced oscillations in response to both agonists. In most cells, the receptor-mediated [Ca2+]i oscillations continued for several minutes in the absence of extracellular Ca2+, although the amplitude of the individual peaks gradually decreased. The activation of [Ca2+]i oscillations by H1-receptors was more dependent upon extracellular Ca2+ than those elicited by alpha 1-receptors, reflecting the greater dependency of the histaminergic response on Ca2+ influx. Readdition of Ca2+ to the incubation buffer resulted in the resumption of the [Ca2+]i oscillations. These results indicate that considerable cycling of Ca2+ between the cytoplasm and the endoplasmic reticulum must occur. Receptor-mediated [Ca2+]i oscillations were much more prevalent in subconfluent cells than in confluent cells, possibly due to increased coupling of the cells at higher densities. The cells were capable of responding independently of one another, since sister cells displayed unique temporal responses immediately following cell division. Thus, the linkage of receptor occupancy to [Ca2+]i elevation is a functionally unique property for each individual cell and can be influenced by epigenetic factors.

Adrenergic alpha-Agonists↗

PubMed1984

Chlorination of endogenous amines by isolated neutrophils. Ammonia-dependent bactericidal, cytotoxic, and cytolytic activities of the chloramines.

Isolated human neutrophilic leukocytes were stimulated to produce hydrogen peroxide (H2O2) and to secrete cytoplasmic granule components including myeloperoxidase into the medium. Myeloperoxidase catalyzed the oxidation of chloride (Cl-) by H2O2 to yield hypochlorous acid (HOCl), which reacted with endogenous nitrogen compounds to yield derivatives containing nitrogen-chlorine (N-Cl) bonds. Compounds available for reaction with HOCl were ammonia (NH+4), taurine, alpha-amino acids, and granule proteins and peptides that were released into the medium. A portion of the N-Cl derivatives formed under these conditions accumulated in the extracellular medium. These long lived oxidizing agents were characterized as hydrophilic, low molecular weight, mono-N-chloramine (RNHCl) derivatives based on their absorption spectrum, ability to oxidize 5-thio-2-nitrobenzoic acid and to chlorinate ammonia (NH+4), and behavior upon ultrafiltration, gel chromatography, and extraction with organic solvents. The RNHCl derivatives were of low toxicity, but reacted with NH+4 to yield the lipophilic oxidizing agent monochloramine (NH2Cl). Therefore, the addition of NH+4 conferred bactericidal, cytotoxic, and cytolytic activities on the RNHCl derivatives. The results indicate that taurine and other neutrophil amines protect neutrophils and other cells against oxidative attack by acting as a trap for HOCl and by competing with endogenous NH+4 for reaction with HOCl. However, the RNHCl derivatives act as a reserve of oxidizing equivalents that is converted to a toxic form when an increase in NH+4 concentration favors formation of NH2Cl.

Amines↗

PubMed2005

Effect of glutathione on UV induction of prophage lambda.

The effect of glutathione (GSH) on the ultraviolet (UV) induction of lambda prophage was investigated in lysogenic Escherichia coli. The data showed that extracellular GSH could inhibit the UV induction of lambda prophage. The inhibitory rates were concentration dependent, and the maximal rate obtained was 94% with 3.0 M GSH. The effect was also measured in three different lambda lysogens: a wild-type strain (wt), an isogenic GSH-deficient strain, and an isogenic strain producing increased amounts of GSH. The result showed that when subjected to UV irradiation (254 nm, 60 J m(-2)), GSH-deficient strain was approximately fivefold more sensitive to be lysed than wt, whereas the strain with higher intracellular GSH levels was only 28% susceptible to be lysed. With electron spin resonance and spin trapping techniques, we observed that free radical signals occurred in the suspensions of UV irradiated lysogenic cells and the intensity of signals was influenced by GSH levels. These results indicate that GSH can significantly inhibit the UV induction of lambda prophage, and that this effect is correlated to its capacity to scavenge free radicals generated after UV irradiation.

Bacteriophage lambda↗

PubMed2005

Generation of free radicals during decomposition of hydroperoxide in the presence of myeloperoxidase or activated neutrophils.

It was shown with the spin trap alpha-(4-pyridyl-1-oxide)-N-tert-butylnitrone that myeloperoxidase (MPO) in the presence of its substrates H2O2 and Cl- as well as activated neutrophils destroy tert-butyl hydroperoxide producing two adducts of O-centered radicals which were identified as peroxyl and alcoxyl radicals. Inhibitory analysis performed with traps of hypochlorite (taurine and methionine), free radical scavengers (2,6-di-tret-butyl-4-methylphenol and mannitol), and MPO inhibitors (salicylhydroxamic acid and 4-aminobenzoic acid hydrazide) revealed that the destruction of the hydroperoxide group in the presence of isolated MPO or activated neutrophils was directly caused by the activity of MPO: some radical intermediates appeared as a result of the chlorination cycle of MPO at the stage of hypochlorite generation, whereas the other radicals were produced independently of hypochlorite, presumably with involvement of the peroxidase cycle of MPO. The data suggest that the activated neutrophils located in the inflammatory foci and secreting MPO into the extracellular space can convert hydroperoxides into free radicals initiating lipid peroxidation and other free radical reactions and, thus, promoting destruction of protein-lipid complexes (biological membranes, blood lipoproteins, etc.).

Catalysis↗

PubMed1993

The torso receptor localizes as well as transduces the spatial signal specifying terminal body pattern in Drosophila.

Specification of the end portions of the Drosophila body depends on the torso (tor) protein, a receptor tyrosine kinase that accumulates uniformly along the entire surface of the embryo but is activated only in the vicinity of the poles. Several genes are normally required for activating tor and appear to define a system in which a gene product tethered to the extracellular vitelline membrane at each end of the egg provides a local source for an extracellular tor ligand. This ligand would have to diffuse from the membrane to the cell surface of the embryo without losing its spatial localization. Here we report that the failure to accumulate tor protein at one or both poles leads to spatially inappropriate activity of more centrally located receptor. This ectopic activity depends on the same gene functions normally required for activating tor; thus we infer that it reflects inappropriate diffusion of the ligand to more central regions of the body. We conclude that the receptor not only transduces the spatial signal imparted by the tor ligand, but also ensures its correct localization by sequestering the ligand. Ligand trapping by receptor may also localize spatial signals in other patterning systems, including specification of the dorsal-ventral axis in Drosophila and of vulval cell fates in Caenorhabditis elegans.

Animals↗

PubMed2000

Preliminary communication. MRNA expression of MT1-MMP, MMP-9, cathepsin K, and TRAP in highly enriched osteoclasts cultured on several matrix proteins and ivory surfaces.

We demonstrated that the transcriptional expression of MT1-MMP, MMP-9, cathepsin K, and TRAP in highly enriched osteoclasts were regulated by different matrix proteins that bind to integrin on osteoclast, such as collagen type I (CoI), fibronectin (FN), vitronectin (VN), osteopontin (OPN), and ivory. Results suggested that the OPN-integrin alphavbeta3 binding plays a more important role than CoI-alpha2beta1 binding in the regulation of osteoclast activity.

Animals↗

PubMed2004

Analysis of secreted proteins during conidial germination of Aspergillus oryzae RIB40.

To broaden our understanding of extracellular proteins of Aspergillus oryzae at the conidial germination stage, analyses of the secreted proteins during germination were carried out. Taka-amylase A (TAA), glucoamylase (GLAA), and aspergillopepsin A (PEPA) were identified as the main products by peptide mass fingerprinting. TAA and PEPA were detected simultaneously with the formation of germ tubes. With the development of germination, the pH of the medium fell from 5.5 to 3.5. The secreted PEPA had a pro-sequence and likely shifted from 42 kDa to 41 kDa below pH 4.6, indicating that the precursor of PEPA was secreted and underwent pH-dependent processing. Furthermore, the 41 kDa protein was trapped by the addition of pepstatin A, the specific inhibitor of PEPA, suggesting that the maturation of pro-PEPA was a stepwise autoprocessing upon acidification of the medium and itself was an intermediate of the processing. It was implied that PEPA plays an important role at the early germination stage.

Aspartic Acid Endopeptidases↗

PubMed2002

The role of the N-terminal propeptide of the pro-aminopeptidase processing protease: refolding, processing, and enzyme inhibition.

Pro-aminopeptidase processing protease (PA protease) is an extracellular zinc metalloprotease produced by Aeromonas caviae T-64 and it is classified as M04.016 according to the MEROPS database. The precursor of PA protease consists of four regions; a signal peptide, an N-terminal propeptide, a C-terminal propeptide, and the mature PA protease. The in vitro refolding of the intermediate pro-PA protease containing the C-terminal propeptide (MC) was investigated in the presence and absence of the N-terminal propeptide. The results indicate that the noncovalently linked N-terminal propeptide is able to assist in the refolding of MC. In the absence of the N-terminal propeptide, MC is trapped into a folding competent state that is converted into the active form by the addition of the N-terminal propeptide. Moreover, the N-terminal propeptide was found to form a complex with the folded MC and inhibit further processing of MC into the mature PA protease. Inhibitory activity of the purified N-terminal propeptide toward mature PA protease was also observed, and the mode of this inhibition was determined to be a mixed, noncompetitive inhibition with an associated allosteric effect.

Aeromonas↗

PubMed2004

Dwarfism and impaired gut development in insulin-like growth factor II mRNA-binding protein 1-deficient mice.

Insulin-like growth factor II mRNA-binding protein 1 (IMP1) belongs to a family of RNA-binding proteins implicated in mRNA localization, turnover, and translational control. Mouse IMP1 is expressed during early development, and an increase in expression occurs around embryonic day 12.5 (E12.5). To characterize the physiological role of IMP1, we generated IMP1-deficient mice carrying a gene trap insertion in the Imp1 gene. Imp1(-/-) mice were on average 40% smaller than wild-type and heterozygous sex-matched littermates. Growth retardation was apparent from E17.5 and remained permanent into adult life. Moreover, Imp1(-/-) mice exhibited high perinatal mortality, and only 50% were alive 3 days after birth. In contrast to most other organs, intestinal epithelial cells continue to express IMP1 postnatally, and Imp1(-/-) mice exhibited impaired development of the intestine, with small and misshapen villi and twisted colon crypts. Analysis of target mRNAs and global expression profiling at E12.5 indicated that Igf2 translation was downregulated, whereas the postnatal intestine showed reduced expression of transcripts encoding extracellular matrix components, such as galectin- 1, lumican, tenascin-C, procollagen transcripts, and the Hsp47 procollagen chaperone. Taken together, the results demonstrate that IMP1 is essential for normal growth and development. Moreover, IMP1 may facilitate intestinal morphogenesis via regulation of extracellular matrix formation.

Animals↗

PubMed1997

Precise analyses of the structure of the thymus for establishing details of the mechanisms underlying thymocyte proliferation and maturation.

Details of thymocyte proliferation and maturation are important for understanding the variability of T cell functions. The following aspects need to be clarified in this context: 1) Ascertaining why hematopoietic committed pre-T cells migrating in the blood stream are trapped and proliferate in the subcapsular region of the thymus. Further morphological and functional studies of stromal cells in situ in the thymus should be conducted. The factors responsible for thymocyte proliferation should be also analysed. 2) How phenotypic maturation of thymocytes takes place and how T-cell receptor (TCR) expression is processed and controlled. 3) Subsequently, how does the selection of thymocytes take place? Is negative selection in fact responsible for the unresponsiveness of the body to self antigens? Further morphological analyses of thymic epithelial cells, thymocytes themselves and macrophages need to be conducted, together with immunohistochemical analyses using many monoclonal antibodies directed against these cells and the extracellular matrix, in order to analyse the cellular dynamics and cell-to-cell interactions occurring in thymus tissues in situ. 4) How mature thymocytes migrate to the periphery: Perivascular structures and the cells accumulating in this space should be intensively analysed morphologically and phenotypically. Lymphatic structures related to the thymus tissues also remain to be studied. To understand these questions, several useful experimental systems can also be employed: 1) Phylogenetical analyses, 2) ontogenical analyses, 3) thymus tissues regenerating from radiation or thymotoxic drugs, 4) thymomas, and 5) thymus tissues from transgenic animals. These important problems could be further studied in such experimental models both morphologically and immunohistochemically, since many useful tools are now available for studies of phenotypic and other markers of thymocytes and thymic epithelial cells. Subsequently, further detailed analyses of thymic structures may shed more light on the mechanisms underlying thymocyte proliferation and maturation.

Animals↗

PubMed2006

Antioxidant therapeutic targets in COPD.

Oxidative stress and chronic inflammation are important features in the pathogenesis of chronic obstructive pulmonary disease (COPD). Oxidative stress has important consequences for several elements of lung physiology and for the pathogenesis of COPD, including oxidative inactivation of antiproteases and surfactants, mucus hypersecretion, membrane lipid peroxidation, alveolar epithelial injury, remodeling of extracellular matrix, and apoptosis. Therefore, targeting oxidative stress with antioxidants or boosting the endogenous levels of antioxidants is likely to be beneficial in the treatment of COPD. Antioxidant and/or anti-inflammatory agents such as thiol molecules (glutathione and mucolytic drugs, such as N-acetyl-L-cysteine and N-acystelyn), dietary polyphenol (curcumin-diferuloylmethane, a principal component of turmeric), resveratrol (a flavanoid found in red wine), green tea (theophylline and epigallocatechin-3- gallate), ergothioneine (xanthine and peroxynitrite inhibitor), quercetin, erdosteine and carbocysteine lysine salt, have been reported to control NF-kappaB activation, regulation of glutathione biosynthesis genes, chromatin remodeling and hence inflammatory gene expression. Specific spin traps such as alpha-phenyl-N-tert-butyl nitrone, a catalytic antioxidant (ECSOD mimetic), manganese (III) meso-tetrakis (N,N'-diethyl-1,3-imidazolium-2-yl) porphyrin (AEOL 10150 and AEOL 10113), and a SOD mimetic M40419 have also been reported to inhibit cigarette smoke-induced inflammatory responses in vivo. Since a variety of oxidants, free radicals and aldehydes are implicated in the pathogenesis of COPD it is possible that therapeutic administration of multiple antioxidants will be effective in the treatment of COPD. Various approaches to enhance lung antioxidant capacity and clinical trials of antioxidant compounds in COPD are discussed.

Animals↗

PubMed2004

Role of peg formation in clamp cell fusion of homobasidiomycete fungi.

In most filamentous basidiomycetes, clamp cells are found at the septa of dikaryotic mycelia. Clamp cell formation starts at hyphal tip cells with the development of a lateral bulge at a position slightly apical to the future septum. Relative to the growth direction of the hypha, the protrusion expands backwards into a hook-like structure. Next, the two genetically different haploid nuclei within the hyphal tip cell divide. A septum appears between clamp cell and hyphal tip cell, thereby trapping one nucleus within the clamp cell. Another septum is laid within the hypha, separating a nucleus of the other type in the newly generated subapical hyphal cell from the two different nuclei kept together in the new apical hyphal cell. Through fusion of clamp and subapical cell, the two solitary nuclei become united within the subapical hyphal compartment. In 1933, Buller described subapical formation of a peg to which the clamp cell fuses as an additional, subsequently neglected step in this series of events. In this study, we represent evidence for subapical peg formation and its role in clamp cell fusion. Our observations potentially indicate a B mating type regulated extracellular communication between clamp and subapical hyphal cell.

Agaricales↗

PubMed2002

Effect of liquid depth on the synthesis and oxidation of nitric oxide in macrophage cultures.

The effect of liquid depth on the synthesis of NO and O(2)(-) was studied in murine macrophage-like RAW 264.7 cells activated by bacterial lipopolysaccharide and interferon-gamma. Rates of NO(2)(-) and NO(3)(-) accumulation were determined 8-11 h after stimulation. The rate of NO synthesis was computed by using a reaction-diffusion model to correct NO(2)(-) and NO(3)(-) accumulation for physical loss of NO, whereas O(2)(-) synthesis was equated with NO(3)(-) formation. Rates of O(2)(-) synthesis determined by a spectrophotometric (cytochrome c) assay were in good agreement with those from NO(3)(-) accumulation and showed production of O(2)(-) to be detectable immediately, in contrast to the approximately 6 h time lag for NO. The assumption that NO(2)(-) and NO(3)(-) are stable end products of the extracellular oxidation of NO by O(2) and O(2)(-), respectively, was supported by the fact that NO(2)(-) and NO(3)(-) concentrations remained constant in the presence of unstimulated cells or stimulated cells where NO synthesis was inhibited. Data were obtained for media depths ranging from 1 to 4 mm. The physical loss of NO was found to be quite significant, exceeding NO(2)(-) and NO(3)(-) accumulation by an order of magnitude at the smallest depth. The principal finding was that the rates of NO(2)(-) and NO(3)(-) accumulation each remained nearly constant over the 4-fold range of liquid depths. Because greater depths should greatly facilitate the trapping of NO as NO(2)(-), this implies that NO synthesis decreased markedly with increasing depth. In contrast, O(2)(-) synthesis remained approximately constant. Oxygen availability is likely to have affected NO synthesis, in that diffusional limitations will yield the lowest cellular O(2) concentrations when the liquid depth is greatest and NO synthesis is known to decrease when O(2) levels are reduced. Concentrations of NO near the cells were calculated to remain at approximately 1 microM for all conditions examined, suggesting that regulation of NO synthase activity by NO might also have mediated the effect of liquid depth.

Animals↗

PubMed1988

Effects of emboli, positive-pressure ventilation, and airway water on lung water measurements.

We tested the effects of microemboli, continuous positive-pressure ventilation (CPPV), and aspirated airway water on measurements of extravascular lung water by use of the technique of thermal indicator dilution (ETVL). A control group of dogs and a group of dogs in which dextran was infused created all levels of pulmonary edema. In an emboli group 0.125 g/kg of starch microemboli (63-74 micron diam) were infused. In groups with emboli and CPPV, starch emboli were infused and CPPV was then applied at 15 cmH2O. In an airway saline group measured amounts of saline were poured into the airway. In all groups postmortem pulmonary extravascular tissue weight (PETW) was determined and compared with the last ETVL. Emboli created an increased scatter when the last ETVL is compared with PETW because 1) blood trapped distal to emboli was included in the ETVL measurement, and/or 2) diffusion limitations for the thermal indicator were exceeded. Emboli and CPPV decreased ETVL/PETW. Airway saline (80 +/- 5%) was measured by ETVL. In conclusion, the ETVL technique is reliable in well-perfused lungs but loses accuracy in measuring lung water after emboli of any size or with large amounts of airway fluid.

Algorithms↗

PubMed1991

Ultrastructural localization of tartrate-resistant acid phosphatase (purple acid phosphatase) activity in chicken cartilage and bone.

Tartrate-resistant acid adenosine triphosphatase activity at pH 6.5, using a lead-salt method, was localized at light and electron microscopic levels in cartilage and bone matrices, osteoclasts, and chondroclasts. Cartilage matrix staining occurred after vascular invasion of the growth plate. In osteoclasts, activity was present in lysosomes, extracellular ruffled border channels, and the underlying cartilage and bone matrices. Staining artifacts occurred at lower pH levels (pH 5.4, 5.0). Adenosine diphosphate, p-nitrophenylphosphate, thiamine pyrophosphate, and alpha-naphthylphosphate also acted as substrates; but no activity was observed when adenosine monophosphate, adenylate-(beta, gamma-methylene) diphosphate, and beta-glycerophosphate were used. The activity was inhibited by NaF, dithionite, and a high concentration of p-chloromercuribenzoic acid, and activated by simultaneous addition of FeCl2 and ascorbic acid, as has been shown in biochemical studies. These histochemical results support the view that the adenosine triphosphate hydrolyzing activity at pH 6.5 is due to tartrate-resistant acid phosphatase (TRAP). There were some differences in ultrastructural localization between TRAP and tartrate-sensitive acid phosphatase (TSAP) activities in osteoclasts: TSAP activity was more intense in lysosomes and Golgi complexes and TRAP was stronger in the cartilage and bone matrices. It is suggested, therefore, that most of TRAP is in an inactive form in cells and is activated when secreted.

Acid Phosphatase↗

PubMed2005

Production, partial characterization and mass spectrometric studies of the extracellular laccase activity from Fusarium proliferatum.

Benzyl alcohol and starch-free commercial wheat bran were effective inducers of the laccase activity in cultures of Fusarium proliferatum (MUCL 31970). Initial pH value in the cultures was also an overriding factor for increasing its production. By gel permeation high-performance liquid chromatography, the enzyme eluted as an apparently homogeneous peak with a molecular mass of 54 kDa, but by isoelectrofocusing, two proteins with pI values of 5.17 and 5.07 were revealed. Two different phenoloxidase activities were also detected after nondenaturing polyacrylamide gel electrophoresis. By matrix-assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-TOF-MS), both proteins showed unique fingerprints, so they were classifiable as isozymes, and were named laccase 1 (Lac1, pI 5.17) and laccase 2 (Lac2, pI 5.07). No clear matches were found when compared with other proteins. The tandem mass spectrometry of some peptides from both isozymes reanalyzed by nanoelectron ionization-ion trap-mass spectrometry (nESI-IT-MS) confirmed their unique character. The following interesting properties, particularly its stability at alkaline pH, make this laccase a promising industrial enzyme for biotechnological applications: maximum activity at 60 degrees C, thermal stability for 2 h at 40 degrees C, optimum pH 3.5 (km=62 microM) measured on 2,2'-azino-bis(3-ethylbenz-thiazoline-6-sulfonate), and pH stability 4-8 (75% stability at pH levels 2.2 and 9) for 2 h at 25 degrees C.

Amino Acid Sequence↗