Relevant bibliographies by topics / Haemolytic activity

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Academic literature on the topic 'Haemolytic activity'

Author: Grafiati
Published: 4 June 2021
Last updated: 13 June 2025

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Journal articles on the topic "Haemolytic activity"

1

Takeda, Kein, Yoshikazu Tanaka та Jun Kaneko. "The N-terminal amino-latch region of Hlg2 component of staphylococcal bi-component γ-haemolysin is dispensable for prestem release to form β-barrel pores". Journal of Biochemistry 168, № 4 (2020): 349–54. http://dx.doi.org/10.1093/jb/mvaa052.

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Abstract The contribution of N-terminal regions of staphylococcal bi-component γ-haemolysin toxin components to haemolytic activity towards human erythrocyte cells was investigated in this study. A deletion construct of N-terminal amino acids 1–10 of Hlg2 (Hlg2 ΔN10), which is the S-component protein of γ-haemolysin, had little effect on its haemolytic activity, whereas N-terminal 1–11 amino acid deletion (Hlg2 ΔN11) significantly delayed haemolysis. Moreover, a deletion of N-terminal amino acids 1–17 of LukF, which is the F-component protein of γ-haemolysin, increased its haemolytic activity in combination with either the wild-type or Hlg2 ΔN10. Unlike the N-terminal amino-latch region of staphylococcal α-haemolysin, which is a single component β-barrel pore-forming toxin, the N-terminal regions present in γ-haemolysin components are dispensable for the haemolytic activity of the bi-component toxin. These results strengthen our recent proposal that staphylococcal bi-component γ-haemolysin toxin uses an N-terminal amino-latch independent molecular switch for prestem release during the formation of β-barrel pores.
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2

Avila-Campos, Mario Julio. "Haemolytic activity of Actinobacillus actinomycetemcomitans strains on different blood types." Revista do Instituto de Medicina Tropical de São Paulo 37, no. 3 (1995): 215–17. http://dx.doi.org/10.1590/s0036-46651995000300006.

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Haemolytic activity of sixty nine Actinobacillus actinomycetemcomitans strains on different animal and human blood types was examined by using a trypticase soy agar supplemented with yeast extract (0.5%). Blood types used were: rabbit, sheep and human (A, Rh+; A, Rh-; B, Rh+; B, Rh-; O, Rh+; O, Rh-; AB, Rh+; AB, Rh- groups). Plates were inoculated and, incubated in microaerophilic conditions, at 37ºC, for 48 h. The haemolytic activity of the tested strains was characterized as alpha-haemolysis. Only two isolates were not haemolytic on all blood types (2.9%), two strains were haemolytic only on human blood (one strain on AB, Rh+ group and another one on A, Rh+ and AB, Rh+ groups). No specificity between haemolysin produced by the tested strains and blood type was observed.
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3

Karunakaran, T., and B. G. Devi. "Characterisation of haemolytic activity fromAeromonas caviae." Epidemiology and Infection 112, no. 2 (1994): 291–98. http://dx.doi.org/10.1017/s0950268800057708.

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SUMMARYAeromonas caviae, an enteropathogen associated with gastroenteritis, displays several virulence characteristics. Studies on the kinetics of growth ofA. caviaeand expression of β–haemolytic toxin revealed thatA. caviaeproduced maximum haemolytic activity extracellularly during the stationary phase. Preliminary studies on the properties ofA. caviaehaemolysin suggested that divalent cations (Mg2+and Ca2+) and thiol compounds, dithiothreitol and mercaptoethanol enhanced the haemolytic activity. Addition of L–cysteine, glutathione and EDTA reduced the haemolytic activity. The iron chelator, 2–2' bipyridyl, significantly inhibited the growth ofA. caviaepossibly by iron limitation, with parallel enhancement of haemolysin production compared toA. caviaegrown in excess of iron. These results suggest thatA. caviaeproduces only β-haemolysin, which resembles the haemolysins reported for several other bacteria and the activity might be regulated by environmental factors especially iron.
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4

Tabata, Atsushi, Yuji Sato, Kentaro Maya та ін. "A streptolysin S homologue is essential for β-haemolytic Streptococcus constellatus subsp. constellatus cytotoxicity". Microbiology 160, № 5 (2014): 980–91. http://dx.doi.org/10.1099/mic.0.075580-0.

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Streptococcus constellatus is a member of the Anginosus group streptococci (AGS) and primarily inhabits the human oral cavity. S. constellatus is composed of three subspecies: S. constellatus subsp. constellatus (SCC), S. constellatus subsp. pharyngis and the newly described subspecies S. constellatus subsp. viborgensis. Although previous studies have established that SCC contains β-haemolytic strains, the factor(s) responsible for β-haemolysis in β-haemolytic SCC (β-SCC) has yet to be clarified. Recently, we discovered that a streptolysin S (SLS) homologue is the β-haemolytic factor of β-haemolytic Streptococcus anginosus subsp. anginosus (β-SAA), another member of the AGS. Furthermore, because previous studies have suggested that other AGS species, except for Streptococcus intermedius, do not possess a haemolysin(s) belonging to the family of cholesterol-dependent cytolysins, we hypothesized that, as with β-SAA, the SLS homologue is the β-haemolytic factor of β-SCC, and therefore aimed to investigate and characterize the haemolytic factor of β-SCC in the present study. PCR amplification revealed that all of the tested β-SCC strains were positive for the sagA homologue of SCC (sagA SCC). Further investigations using β-SCC strain W277 were conducted to elucidate the relationship between sagA SCC and β-haemolysis by constructing sagA SCC deletion mutants, which completely lost β-haemolytic activity. This loss of β-haemolytic activity was restored by trans-complementation of sagA SCC. Furthermore, a co-cultivation assay established that the cytotoxicity of β-SCC was clearly dependent on the presence of sagA SCC. These results demonstrate that sagA SCC is the factor responsible for β-SCC β-haemolysis and cytotoxicity.
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5

Dailey, D. C., C. Te-Hung, and J. F. Alderete. "Characterization ofTrichomonas vaginalishaemolysis." Parasitology 101, no. 2 (1990): 171–75. http://dx.doi.org/10.1017/s0031182000063204.

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The haemolytic activity of liveTrichomonas vaginalisorganisms was investigated. Optimal haemolysis of human erythrocytes was observed at a parasite to erythrocyte ratio of 1:5 during a 2 h incubation period. No haemolytic activity was detected in concentrated culture supernatants after overnight growth of trichomonads or when parasites were separated from erythrocytes by a 3 μm filter, suggesting a contact-dependent mechanism for haemolysis. The haemolytic activity was temperature-dependent and maximal haemolysis occurred at 37 °C. Treatment of trichomonads with metronidazole reduced levels of haemolysis by > 50%. Maximal haemolysis occurred at the pH range of the vagina during trichomoniasis.N-μ-tosyl-L-lysyl-chloromethyl ketone and iodoacetamide, inhibitors of trichomonad cysteine proteinases, reduced the haemolytic activity of live parasites.
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6

Hasegawa, Hiroaki, and Claudia C. Häse. "The extracellular metalloprotease of Vibrio tubiashii directly inhibits its extracellular haemolysin." Microbiology 155, no. 7 (2009): 2296–305. http://dx.doi.org/10.1099/mic.0.028605-0.

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Vibrio tubiashii is a re-emerging pathogen of molluscs that secretes a variety of extracellular products (ECPs), including a metalloprotease and a cytolysin/haemolysin. Previously, we reported that the V. tubiashii haemolysin locus consists of two ORFs (vthB and vthA), similar to that of the homologous haemolysin genes (vvhB and vvhA) found in Vibrio vulnificus. Here, we demonstrate that the concomitant expression of both V. tubiashii genes resulted in significantly higher haemolytic activity than the vthA gene alone. In addition, we created a VthAB− mutant strain of V. tubiashii that was virtually devoid of haemolytic activity in liquid media. Interestingly, significant production of an additional haemolysin(s) was observed on blood plates. Moreover, we have previously reported that in V. tubiashii, proteolytic and haemolytic activities are inversely produced during bacterial growth. Here, we study this correlation in more detail and present evidence that the VtpA metalloprotease inhibits haemolytic activity in culture supernatants, based on the following evidence: (i) loss of metalloprotease activity by either mutation or EDTA inhibition resulted in increased haemolytic activity; (ii) overexpression of the vtpA gene resulted in decreased haemolytic activity; (iii) purified VtpA metalloprotease directly diminished haemolytic activity by purified VthA haemolysin. Importantly, we found not only that vthAB gene expression remained high throughout growth but also that there were no dramatic differences in vthAB gene expression between the parent and VtpA− mutant strains. Thus, our results strongly suggest that the V. tubiashii metalloprotease directly targets its haemolysin.
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7

Ahsan, Chowdhury Rafiqul, Farah Shamma, Nazmul Ahsan, and Moutusee Jubaida Islam. "Environmental Factors Regulate the hlyE Gene Expression in Both S. typhi and E. coli in a Similar Way to Display Haemolytic Activity." Bangladesh Medical Research Council Bulletin 42, no. 1 (2017): 33–38. http://dx.doi.org/10.3329/bmrcb.v42i1.32001.

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Haemolysin (HlyE) is an essential virulence factor of Salmonella, Escherichia coli and other enteric bacteria. Although, a substantial degree of haemolytic activity is not seen under normal culture conditions in these organisms, however, the non-haemolytic E. coli K-12 showed significant haemolytic activity under stress conditions. To confirm this phenomenon in other enteric bacteria, in this study, the production of haemolysin in Salmonella enterica serovar Typhi under stress conditions, like oxygen and glucose starvations in vitro was investigated during March-December 2015. For this, S. typhi was cultured under oxygen or glucose starvation condition separately and this organism showed high haemolytic activity. The activity was found to be much higher when both the conditions were applied together. Also, the role of the transcription factor SlyA of S. typhi was investigated on induction of haemolytic activity. When E. coli K-12 was transformed with plasmid containing the gene of SlyA, the recombinant bacteria without any starvation condition, also showed similar haemolytic activity that was exhibited by S. typhi grown under oxygen and glucose starvation conditions. All these findings suggest that both environmental factors like oxygen or glucose starvation and overexpression of the transcription factor SlyA have important role in inducing hlyE gene expression in S. typhi.
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8

CHEN, Desong, R. Manjunatha KINI, Raymond YUEN, and Hoon Eng KHOO. "Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom: pore formation and the role of cationic amino acid residues." Biochemical Journal 325, no. 3 (1997): 685–91. http://dx.doi.org/10.1042/bj3250685.

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Stonustoxin (SNTX) is a two-subunit protein toxin purified from the venom of the stonefish (Synanceja horrida), which induces potent haemolytic activity. We examined the pore-forming property of this non-enzymic protein by an osmotic protection assay. SNTX-induced haemolysis was completely prevented by osmotic protectants of adequate size [poly(ethylene) glycol 3000; molecular diameter approx. 3.2 nm]. Uncharged molecules of smaller size, such as raffinose and poly(ethylene) glycol 1000–2000, failed to protect against cell lysis. These findings indicate that SNTX induces the formation of hydrophilic pores in the cell membrane, which results in the lysis of erythrocytes. Since cationic residues contribute significantly to the cytolytic activity of several other pore-forming toxins, we examined the role of positively charged lysine and arginine residues in the haemolytic activity of SNTX. SNTX lost its haemolytic activity when the positively charged side chains of lysine residues were neutralized or converted into negatively charged side chains upon carbamylation or succinylation respectively. The haemolytic activity of SNTX was also inhibited by the modification of positively charged arginine residues using 2,3-butanedione. The loss of haemolysis showed strong correlation with the number of Lys or Arg residues modified. CD analyses, however, showed that the conformation of SNTX was not significantly affected by these chemical modifications. Further, the haemolytic activity of SNTX was competitively inhibited by various negatively charged lipids, such as phosphatidylserine, cardiolipin and monosialogangliosides. These results indicate that SNTX induces potent haemolytic activity through the formation of pores in the cell membrane, and that cationic residues play a crucial role in its cytolytic mechanism.
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9

Green, Sarah, Erica Partridge, Edore Idedevbo, and Anton Borg. "Steroid Refractory Autoimmune Haemolytic Anaemia Secondary to Sarcoidosis Successfully Treated with Rituximab and Mycophenolate Mofetil." Case Reports in Hematology 2016 (2016): 1–4. http://dx.doi.org/10.1155/2016/9495761.

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Autoimmune haemolytic anaemia is not a well-recognised complication of sarcoidosis. We describe the case of a 30-year-old female who presented with acute warm haemolytic anaemia and widespread lymphadenopathy. Sarcoidosis was diagnosed on lymph node biopsy and further investigation. The haemolytic anaemia responded only to a high dose of steroids. Evidence regarding treatment of steroid refractory autoimmune haemolysis secondary to sarcoidosis is lacking. Based on the emergent evidence that both disorders share common immunopathogenic mechanisms involving Th1 and Th17 lymphocytes, our patient was given rituximab and mycophenolate mofetil to successfully suppress the haemolysis and sarcoid activity.
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10

Papi, M., M. C. Lauriola, V. Palmieri, G. Ciasca, G. Maulucci, and M. De Spirito. "Plasma protein corona reduces the haemolytic activity of graphene oxide nano and micro flakes." RSC Advances 5, no. 99 (2015): 81638–41. http://dx.doi.org/10.1039/c5ra15083c.

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GO flakes, able to disrupt the erythrocyte plasma membrane, greatly reduce their haemolytic activity after interacting with plasma proteins. Haemolysis activity increases inversely to the GO flakes size.
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