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RISS 인기검색어
- 검색키워드
- 저자 : Kartikasari,Apriliana E.R. (검색결과 11 건)
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Expression in Escherichia coli of a Putative Human Acetohydroxyacid Synthase
Duggleby, Ronald G.,Kartikasari, Apriliana E.R.,Wunsch, Rebecca M.,Lee, Yu-Ting,Kil, Mee-Wha,Shin, Ju-Young,Chang, Soo-Ik Korean Society for Biochemistry and Molecular Biol 2000 Journal of biochemistry and molecular biology Vol.33 No.3
A human gene has been reported that may encode the enzyme acetohydroxyacid synthase. Previously this enzyme was thought to be absent from animals although it is present in plants and many microorganisms. In plants, this enzyme is the target of a number of commercial herbicides and the use of these compounds may need to be reassessed if the human enzyme exists and proves to be susceptible to inhibition. Here we report the construction of several plasmid vectors containing the cDNA sequence for this protein, and their expression in Escherichia coli. High levels of expression were observed, but most of the protein proved to be insoluble. The small amounts of soluble protein contained little or no acetohydroxyacid synthase activity. Attempts to refold the insoluble protein were successful insofar as the protein became soluble. However, the refolded protein did not gain any acetohydroxyacid synthase activity. In vivo complementation tests of an E. coli mutant produced no evidence that the protein is active. Incorrect folding, or the lack of another subunit, may explain the data but we favor the interpretation that this gene does not encode an acetohydroxyacid synthase.
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Expression in Escherichia coli of a Putative Human Acetohydroxyacid Synthase
Chang,Soo-Ik,Kartikasari,Apriliana E.R.,Wunsch,Rebecca M.,Lee,Yu-Ting,Kil,Mee-Wha,Shin,Ju-Young,Duggleby,Ronald G. The Korea Science and Technology Center 2000 BMB Reports Vol.33 No.3
A human gene has been reported that may encode the enzyme acetohydroxyacid synthase. Previously this enzyme was thought to be absent from animals although it is present in plants and many microorganisms. In plants, this enzyme is the target of a number of commercial herbicides and the use of these compounds may need to be reassessed if the human enzyme exists and proves to be susceptible to inhibition. Here we report the construction of several plasmid vectors containing the cDNA sequence for this protein, and their expression in Escherichia coli. High levels of expression were observed, but most of the protein proved to be insoluble. The small amounts of soluble protein contained little or no acetohydroxyacid synthase activity. Attempt to refold the insoluble protein were successful insofar as the protein became soluble. However, the refolded protein did not gain any acetohydroxyacid synthase activity. In vivo complementation tests of an E. coli mutant produced no evidence that the protein is active. Incorrect folding, or the lack of another subunit, may explain the data but we favor the interpretation that this gene does not encode an acetohydroxyacid synthase.
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Occult Amebiasis among Pediatric with Enterocolitis in National Referral Hospital in Indonesia
Inawaty Inawaty,Sari Ika Puspa,Susanto Lisawati,Kartikasari Dwi Peni,Oswari Hanifah,Kurniawan Agnes 대한감염학회 2024 Infection and Chemotherapy Vol.56 No.2
Background Enterocolitis and gastroenteritis remain major health problems, particularly in children living in developing countries. Intestinal protozoa, such as Entamoeba histolytica, Blastocystis, and Cyclospora, are frequently associated with these conditions. Amebic colitis can cause serious complications, including fulminant necrotizing colitis, toxic megacolon, extraintestinal amebiasis, and stunting in children. The diagnosis of amoebiasis is challenging, relying on microscopic examination, which cannot distinguish E. histolytica from the nonpathogenic E. dispar and E. moshkovskii. Therefore, this study aimed to identify intestinal parasites, particularly Entamoeba, their prevalence, and the clinical characteristics of patients admitted for enterocolitis and gastroenteritis at a tertiary-referral hospital. Material and Methods A cross-sectional, retrospective study was conducted at a national, tertiary-referral government hospital, in Jakarta. Of the 111 retrieved medical records from hospitalized patients with enterocolitis and gastroenteritis, for which parasitology feces were examined, 54 fecal samples (48.6%) were still available in the parasitology laboratory storage. All fecal samples underwent the following tests: 1) direct stool examination, after staining with 1% Lugol’s solution, and using the water–ether concentration method; 2) modified acid-fast staining for coccidian parasites; 3) Jones’ culture medium to detect Blastocystis; 4) copro-antigen assay to detect Cryptosporidium and Giardia; and 5) a polymerase chain reaction (PCR) assay to identify Entamoeba. Clinical and demographic data were obtained from the medical records. Results Largely, patients (44.1%) were from the cohort of young children ≤5 years old, followed by adults aged 19–60 years old (24.3%). Both cohorts exhibited polyparasitism. Intestinal parasites were detected in 17 out of the 54 samples (31.4%). These included 6 (11.1%), 2 (3.7%),5 (9.2%), 3 (5.5%), 2 (3.7%), and 1 (1.8%) samples that were positive for Blastocystis, E dispar, E. histolytica, E. moshkovskii, Cryptosporidium, and Dientamoeba fragilis, respectively. PCR analysis revealed that 10 samples were positive for Entamoeba infection, eight of which originated from pediatric patients. Conclusion At a national tertiary-referral hospital in Indonesia, Entamoeba infection was the most prevalent parasite among pediatric patients with enterocolitis. E. histolytica and E. moshkovskii were the two main species identified by PCR. Therefore, PCR assays and fecal occult–blood tests are recommended in cases of enterocolitis and gastroenteritis. Background Enterocolitis and gastroenteritis remain major health problems, particularly in children living in developing countries. Intestinal protozoa, such as Entamoeba histolytica, Blastocystis, and Cyclospora, are frequently associated with these conditions. Amebic colitis can cause serious complications, including fulminant necrotizing colitis, toxic megacolon, extraintestinal amebiasis, and stunting in children. The diagnosis of amoebiasis is challenging, relying on microscopic examination, which cannot distinguish E. histolytica from the nonpathogenic E. dispar and E. moshkovskii. Therefore, this study aimed to identify intestinal parasites, particularly Entamoeba, their prevalence, and the clinical characteristics of patients admitted for enterocolitis and gastroenteritis at a tertiary-referral hospital. Material and Methods A cross-sectional, retrospective study was conducted at a national, tertiary-referral government hospital, in Jakarta. Of the 111 retrieved medical records from hospitalized patients with enterocolitis and gastroenteritis, for which parasitology feces were examined, 54 fecal samples (48.6%) were still available in the parasitology laboratory storage. All fecal samples underwent the following tests: 1) direct stool examination, after staining with 1% Lugol’s solution, and using the water–ether concentration method; 2) modified acid-fast staining for coccidian parasites; 3) Jones’ culture medium to detect Blastocystis; 4) copro-antigen assay to detect Cryptosporidium and Giardia; and 5) a polymerase chain reaction (PCR) assay to identify Entamoeba. Clinical and demographic data were obtained from the medical records. Results Largely, patients (44.1%) were from the cohort of young children ≤5 years old, followed by adults aged 19–60 years old (24.3%). Both cohorts exhibited polyparasitism. Intestinal parasites were detected in 17 out of the 54 samples (31.4%). These included 6 (11.1%), 2 (3.7%),5 (9.2%), 3 (5.5%), 2 (3.7%), and 1 (1.8%) samples that were positive for Blastocystis, E dispar, E. histolytica, E. moshkovskii, Cryptosporidium, and Dientamoeba fragilis, respectively. PCR analysis revealed that 10 samples were positive for Entamoeba infection, eight of which originated from pediatric patients. Conclusion At a national tertiary-referral hospital in Indonesia, Entamoeba infection was the most prevalent parasite among pediatric patients with enterocolitis. E. histolytica and E. moshkovskii were the two main species identified by PCR. Therefore, PCR assays and fecal occult–blood tests are recommended in cases of enterocolitis and gastroenteritis.
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Expression in Escherichia coli of a Putative Human Acetohydroxyacid Synthase
Chang, Soo Ik,Duggleby, Ronald G .,Kil, Mee Wha,Kartikasari, Apriliana E . R .,Wunsch, Rebecca M .,Lee, Yu Ting,Shin, Ju Young 생화학분자생물학회 2001 BMB Reports Vol.33 No.3
A human gene has been reported that may encode the enzyme acetohydroxyacid synthase. Previously this enzyme was thought to be absent from animals although it is present in plants and many microorganisms. In plants, this enzyme is the target of a number of commercial herbicides and the use of these compounds may need to be reassessed if the human enzyme exists and proves to be susceptible to inhibition. Here we report the construction of several plasmid vectors containing the cDNA sequence for this protein, and their expression in Escherichia coli. High levels of expression were observed, but most of the protein proved to be insoluble. The small amounts of soluble protein contained tittle or no acetohydroxyacid synthase activity. Attempts to refold the insoluble protein were successful insofar as the protein became soluble. However, the refolded protein did not gain any acetohydroxyacid synthase activity. In vivo complementation tests of an E. coli mutant produced no evidence that the protein is active. Incorrect folding, or the lack of another subunit, may explain the data but we favor the interpretation that this gene does not encode an acetohydroxyacid synthase.
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Enzymatic hydrolyzation of Cordyceps militaris mushroom extracts and its effect on spent hen chicken
Barido Farouq Heidar,Puruhita,Hertanto Bayu Setya,Cahyadi Muhammad,Kartikasari Lilik Retna,Sujiwo Joko,Kim Juntae,김학연,Jang Aera,이성기 아세아·태평양축산학회 2024 Animal Bioscience Vol.37 No.7
Objective: This study was aimed to investigate the effect of fresh and dried hydrolyzed <i>Cordyceps militaris</i> (CM) mushroom with proteolytic enzymes; bromelain (CMB), flavorzyme (CMF), and mixture of bromelain: flavorzyme (CMBF) on quality properties of spent hen chicken.Methods: Mushroom extract (CME) were combined with three proteolytic enzyme mixtures that had different peptidase activities; stem bromelain (CMB), flavorzyme (CMF), and mixture of stem bromelain:flavorzyme (CMBF) at (1:1). The effect of these hydrolysates was investigated on spent hen breast meat via dipping marination.Results: Hydrolyzation positively alters functional properties of CM protease. in which bromelain hydrolyzed group (CMB) displayed the highest proteolytic activity at 4.57 unit/mL. The antioxidant activity had a significant increment from 5.32% in CME to 61.79% in CMB. A significantly higher emulsion stability index and emulsification activity index compared to CME were another result from hydrolyzation (p<0.05). Texture properties along with the shear force value and myofibrillar fragmentation index were notably improved under CMB and CMBF in fresh condition. Marination with CM mushroom protease that was previously hydrolyzed with enzymes was proven to also increase the nucleotide compounds, indicated by higher adenosine 5’-monophosphate (AMP) and inosine 5’-monophosphate (IMP) in hydrolysate groups (p<0.05). The concentration of both total and insoluble collagen remained unchanged, meaning less effect from CM protease.Conclusion: This study suggested the hydrolyzation of CM protease with bromelain or a mixture of bromelain:flavourzyme to significantly improve functional properties of protease and escalate the taste-related nucleotide compounds and texture profiles from spent hen breast meat. Objective: This study was aimed to investigate the effect of fresh and dried hydrolyzed Cordyceps militaris (CM) mushroom with proteolytic enzymes; bromelain (CMB), flavorzyme (CMF), and mixture of bromelain: flavorzyme (CMBF) on quality properties of spent hen chicken. Methods: Mushroom extract (CME) were combined with three proteolytic enzyme mixtures that had different peptidase activities; stem bromelain (CMB), flavorzyme (CMF), and mixture of stem bromelain:flavorzyme (CMBF) at (1:1). The effect of these hydrolysates was investigated on spent hen breast meat via dipping marination. Results: Hydrolyzation positively alters functional properties of CM protease. in which bromelain hydrolyzed group (CMB) displayed the highest proteolytic activity at 4.57 unit/mL. The antioxidant activity had a significant increment from 5.32% in CME to 61.79% in CMB. A significantly higher emulsion stability index and emulsification activity index compared to CME were another result from hydrolyzation (p<0.05). Texture properties along with the shear force value and myofibrillar fragmentation index were notably improved under CMB and CMBF in fresh condition. Marination with CM mushroom protease that was previously hydrolyzed with enzymes was proven to also increase the nucleotide compounds, indicated by higher adenosine 5’-monophosphate (AMP) and inosine 5’-monophosphate (IMP) in hydrolysate groups (p<0.05). The concentration of both total and insoluble collagen remained unchanged, meaning less effect from CM protease. Conclusion: This study suggested the hydrolyzation of CM protease with bromelain or a mixture of bromelain:flavourzyme to significantly improve functional properties of protease and escalate the taste-related nucleotide compounds and texture profiles from spent hen breast meat.
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