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- 저자 : Kittinan Komolpis (검색결과 4 건)
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Kittinan Komolpis,Chatchawan Udomchokmongkol,Songchan Phutong,Tanapat Palaga 한국공업화학회 2010 Journal of Industrial and Engineering Chemistry Vol.16 No.4
A hybridoma producing monoclonal antibody (MAb) specific for enrofloxacin was cultivated in a 2-L stirred-tank bioreactor in various modes and the performances of each mode were compared. In batch mode, a maximum viable cell and MAb concentration of 9.21 105 cells mL1 and 67.3 mg L1,respectively, were obtained. When the hybridoma was cultivated in a fed-batch culture with the addition of specific nutrients, no improvement in either the viable cell number or MAb concentration was observed. On the other hand, an increase in the production of toxic metabolites, i.e. ammonia and lactate, was observed with growth inhibition of the hybridoma cells occurring at ammonia and lactate concentrations of 2.0 mM and 2.0 g L1, respectively. However, the best performance of hybridoma cultivation was achieved in a perfusion culture mode using a spin filter, which was installed in the stirred-tank reactor as a cell retention device with a perfusion rate of 0.80 vvd. Under these conditions a steady viable cell concentration of 1.57 106 cells mL1 was obtained within five days with an overall productivity and yield of 73.7 mg L1 d1 and 61.4 mg d1, respectively, which was a significant increase over that attained with the batch process.
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Thanyapat Jarupalee,Pantipa Chatchatee,Kittinan Komolpis,Narissara Suratannon,Sittiruk Roytrakul,Yodying Yingchutrakul,Wanaporn Yimchuen,Patcharavadee Butta,Alain Jacquet,Tanapat Palaga 대한천식알레르기학회 2018 Allergy, Asthma & Immunology Research Vol.10 No.1
Purpose: Black tiger shrimp Penaeus monodon is one of the common causes of shellfish allergy that is increasing worldwide. One of the important problems in the management of shellfish allergy is the lack of accurate diagnostic assay because the biological and immunological properties of allergens in black tiger shrimp have not been well characterized. This study aims to detect proteins with the ability to bind and cross-link immunoglobulin E (IgE) from black tiger shrimp by enzyme-linked immunosorbent assay (ELISA), Western blot, and a humanized rat basophilic leukemia reporter cell line RS-ATL8. Methods: Sera from shrimp allergic subjects were subjected to ELISA and Western blots using raw or cooked shrimp extract as antigens. Pooled sera were used to sensitize the RS-ATL8 reporter cell line and cells were activated by shrimp extract. Eluted protein extracts separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) were tested on the RS-ATL8 cell line and subjected to mass spectrometry to identify potential candidate allergens. Results: Allergic sera reacted stronger to raw shrimp extract than cooked shrimp extract (P=0.009). Western blot demonstrated that major IgE reactivity protein bands were at 32-39 kDa and 91-230 kDa in both raw and cooked shrimp extracts. The eluted protein bands at the molecular weight of 38 and 115 kDa from raw shrimp extract induced IgE cross-linking as assayed by the RS-ATL8 cell line. These protein bands were subjected to mass spectrometry for analysis. Ubiquitin-activating enzyme and crustacyanin were identified as potential candidate novel shrimp allergens. Conclusions: The RS-ATL8 reporter cell line can be used to identify potential new shrimp allergens that can functionally cross-link IgE and induce mast cell degranulation.
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Enzymatic hydrolysis of rawhide using papain and neutrase
Siriporn Damrongsakkul,Kongpob Ratanathammapan,Kittinan Komolpis,Wiwut Tanthapanichakoon 한국공업화학회 2008 Journal of Industrial and Engineering Chemistry Vol.14 No.2
Rawhide split was hydrolysed separately by two proteolytic enzymes, papain and neutrase. The effects of enzymatic conditions of the hydrolysis reaction were investigated. During the first 10 min of the enzymatic hydrolysis, the yield of the hydrolysed protein increased sharply, then it slowly increased or became essentially constant due to the limited availability of the substrate. The optimum hydrolysis conditions of papain and neutrase for highest protein yield are at 70 ℃,pH6–7 and 40–50 ℃,pH6–7, respectively. The product frompapain hydrolysis is a gelatin with lowgel strength and viscosity,while that fromneutrase hydrolysis is collagen hydrolysatewith viscosity as lowas water. This is considered to indicate that longer fragments of protein are obtained from papain hydrolysis than that from neutrase implying different mechanisms of papain and neutrase hydrolysis
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Production and Characterization of a Monoclonal Antibody Against Enrofloxacin
( Chusri Manaspong ),( Pitikarn Wongphanit ),( Tanapat Palaga ),( Songchan Puthong ),( Sarintip Sooksai ),( Kittinan Komolpis ) 한국미생물 · 생명공학회 2013 Journal of microbiology and biotechnology Vol.23 No.1
Enrofloxacin is a fluoroquinolone antibiotic approved for the treatment of infections in animals. Because of the side effects to consumers of animal products, the maximum residue limits (MRLs) of enrofloxacin in animal tissues for consumption are regulated. In this study, a monoclonal antibody (mAb) against enrofloxacin was prepared and characterized for the development of a direct competitive enzyme-linked immunosorbent assay (ELISA). The obtained mAb, Enro44, was highly specific for enrofloxacin and had a 50% inhibition concentration (IC50) of 1.99 ng/ml in a competitive ELISA, and the limit of detection (LOD) was 0.50 ng/ml. The cross-reactivity of the mAb with other quinolones and fluoroquinolones was lower than 0.01%. The subclass of the mAb Enro44 was identified as IgG1. The antigen (Ag)-captured direct competitive ELISA using the mAb Enro44 was tested on different spiked samples, including chicken muscle, cattle milk, and cattle urine, and the assay demonstrated recoveries of 82-112%, 80-125%, and 78-124%, respectively. Furthermore, the quantitation of enrofloxacin obtained from the ELISA and from high-performance liquid chromatography (HPLC) was in good agreement, with the linear regression coefficient between 0.933 and 1.056. The cDNAs encoding a heavy-chain Fd fragment (VH and CH1) and a light chain of the mAb Enro44 were cloned and sequenced. Taken together, the results obtained reveal a potential use of this mAb in an ELISA for the detection of enrofloxacin in food samples. The information of amino acid sequence of this mAb will be useful for further modification and production of the mAb in a bioreactor.
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