• Title/Summary/Keyword: specifity

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Validity of Serum Cystatin C for Prediecting Obesity Nephropathy

  • Asefy, Zahra;Amirrasouli, Hooshang;Khoyi, Masood;Hashemi, Vida
    • Interdisciplinary Bio Central
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    • v.4 no.2
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    • pp.4.1-4.4
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    • 2012
  • Background: Serum concentration of cystatin C, a marker of glomerular filtration has been associated with cardiovascular disease (CVD). The aim of this study was to evaluate cystatin C as a marker of obese patients without chronic kidney disease (CKD). Materials and Methods: The study population consisted of 36 subjects with metabolic syndrome and 32 subjects free of metabolic syndrome (the control group). HDL-C, LDL-C, blood urea, triglycerides, glucose, HbA1c, serum cystatin C and serum creatinine were measured in both groups. GFR was calculated in both groups using Cockroft-Gault equation. Results: Obese patients showed higher cystatin C levels than normal samples ($1.28{\pm}0.29$, P < 0.05). In the binary logistic regression, obese patients were significantly associated with elevated cystatin C levels. Conclusion: Our results suggest that cystatin C may be a marker for obese patients and may identify a certain degree of renal dysfunction even when serum creatinine does not exceed the normal level. In this study, we demonstrated that serum creatinineand GFR did not differ significantly between the diabetic and the control groups. Serum concentration of cystatin C was significantly higher in the diabetic group compared with the control group. The strengths of this study are the evaluation of reliability and sensivity in comparison with a 'routine test of GFR'. The methodology used allows an appropriate statistical comparison of reliability in contrast to most other previous evaluations of GFR.

Aberrant Expression of E-cadherin in Lung Tissues of Patients with Probable Lung Cancer

  • Yuan, Yu-Lin;Wang, Yu-Ming;Liu, Hua;Qin, Gui-Fang;Tang, Ai-Guo;Duan, Yong
    • Asian Pacific Journal of Cancer Prevention
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    • v.13 no.10
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    • pp.5149-5153
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    • 2012
  • Introduction: This study assessed the relationship of E-cadherin mRNA and protein expression with the diagnosis of lung cancer with the aim of providing an auxiliary diagnostic method. Methods: Semi-quantitative nested RT-PCR and western blotting were applied to detect E-cadherin mRNA transcripts and protein, respectively, in 30 cases of diagnostic lung cancer, 30 cases of clinically suspected patients with lung cancer and 30 cases of other disease. Immunohistochemical staining was also used to detect E-cadherin. Results: Remarkably decreased levels of relative E-cadherin mRNA value and increased E-cadherin protein negativity were observed in probable lung cancer, when compared with possible lung cancer and others. With a threshold of 1.45, relative E-cadherin mRNA value showed a sensitivity of 90% and a specifity of 83% for the diagnosis of lung cancer. The combination of decreased relative E-cadherin mRNA value and negative E-cadherin protein increased the specificity and sensitivity. Conclusion: These data suggest that Chinese patients with diagnostic lung cancer have similar decreased levels of relative E-cadherin mRNA and E-cadherin protein value in the lung cancer tissues as in lung cancer patients in other countries. Measurement of relative E-cadherin mRNA and protein values in lung cancer tissues has potential for lung cancer diagnosis.

Improvement of ${\beta}-glucosidase$ Activity of Olea europaea Fruit Extracts Processed by Membrane Technology

  • Mazzei, R.;Giomo, L.;Spadafora, A.;Mazzuca, S.;Drioli, E.
    • Korean Membrane Journal
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    • v.8 no.1
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    • pp.58-66
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    • 2006
  • The ${\beta}-glucosidase$ from olive fruit is of particular interest compared to the ones from other sources because it has shown to have high specifity to convert the oleuropein into dialdehydes, which have antibacterial activity and are of high interest for their application in the food and pharmaceutical fields. The enzyme is not yet commercially available and advanced clean and safe technologies for its purification able to maintain the functional stability are foreseen. The purification of this protein from fruit extracts has been already tempted by electrophoresis but either enzyme deactivation or high background with unclear profiles occurred. In this work, fruit extracts obtained from the ripening stage that showed the highest enzyme activity have been processed by diafiltration and ultrafiltration. Asymmetric membranes made of polyamide or polysulphone having 50 and 30 kDa molecular weight cut-off, respectively, were tested for the diafiltration process. Ultrafiltration membranes made of polyethersulfone with 4 kDa molecular weight cut-off were used to concentrate the dia-filtered permeate solutions. The efficiency of the separation processes was evaluated byenzyme activity tests using the hydrolysis of p-D-nitrophenyl-${\beta}$-D-glucopyranoside (pNPGlc) as reaction model. Qualitative and quantitative electrophoresis were applied to analyze the composition of protein solution before and after the membrane separation; in addition dot blot and western blot analyses were applied to verify the presence of ${\beta}-glucosidase$ in the processed fractions. The overall results showed that the ${\beta}-glucosidase$ functional stability was preserved during the membrane operations and the removal of 20 kDa proteins allowed to increase the specific activity of the enzyme of about 52% compared to the one present in the initial fruit extract.

Development of diagnostic kit(Test-MT) for the microplate latex agglutination test of toxoplasmosis in animal (Latex 응집반응을 이용한 동물의 톡소플라즈마병 진단용 kit 개발에 관한 연구)

  • Suh, Myung-deuk;Joo, Hoo-don;Maass, Daivd
    • Korean Journal of Veterinary Research
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    • v.35 no.3
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    • pp.583-593
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    • 1995
  • The present study was conducted to develop a toxoplasma latex agglutination test antigen(Test-MT) and evaluate the toxoplasma latex agglutination(LA) test using a newly-made "Test-MT kit" by comparing with the Toxo-MT kit(Eiken chemical co, Tokyo). Also, the specifity and sensitivity test were made by comparing with IFA test and IgG-ELISA. Tachyzoite suspensions of Toxoplasma gondii(RH strain) were ultracentrifuged for 30min at $60,000{\times}g(4^{\circ}C)$ and the supernatant was used as a water-lysate antigen. Polystyrene latex particles of $1.0{\mu}m$ in diameter(Polyscience co) were used for the preparation of sensitized latex-antigen supension(Test-MT). The frequency distribution of LA titers in Test-MT showed two peaks at <1:32 and 1:128. The borderline titer for positive test in Test-MT was determined to be 1:64. But the frequency distribution of LA tites in Toxo-MT showed two peaks at <1:16 and 1:64. The positive borderline was determined to be 1:32. Agreement of reactions between Test-MT and Toxo-MT kit by LA test was shown 92.5% in bovine sera and 97.0% in swine sera, respectively. From the results obtained here it was determined that the sensitized latex-antigen, Test-MT kit, for the microtiter agglutination test prepared as same as by the procedure described in the previous paper(Suh and Lee, 1993) was useful as a highly specific, sensitive and stable immunotiteration reagent for serodiagnosis of toxoplasma infection in animal sera.

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Studies on the screening and properties of Raw Starch Saccharifying Microorganism(II) - Purification and characterization of raw starch-digesting enzyme from Aspergillus sp. SN-871 - (생전분(生澱粉) 자화성(資化性) 미생물(微生物)의 분리(分離)와 성질(性質)에 관(關)한 연구(硏究)(II) - Aspergillus sp. SN-871이 생산하는 생전분 분해효소의 정제 및 특성 -)

  • Suh, Myung-Ja;Nho, Kyoung-Hee
    • The Korean Journal of Mycology
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    • v.15 no.3
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    • pp.175-182
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    • 1987
  • A raw starch saccharifying enzyme from Aspergillus sp. SN-871 was purified by ammonium sulfate precipitation, DEAE-cellulose column chromatography, CM-Sephadex C-50 column chromatography and Sephadex G-75 gel filtration. The specific activity of purified enzyme was 18 fold and the yeild was 13.40%. The molecular weight of the purified enzyme was estimated as approximately 40,000 dalton by the method of Andrews gel filtration. The optimum pH and temperature for this enzyme were found to be 4 and $40^{\circ}C$, respectively and the stable range of pH was 2 to 5. The enzyme was themostable at below $60^{\circ}C$ and inactivated at $70^{\circ}C$. It showed a tendency to increase the enzyme activity under the presence of 0.01 M $BaCl_2$, but under 0.01 M$Pb(NO_3)_2$, $AgSO_4$, and $K_3Fe(CN)_6$ and citric acid etc. inhibited it completely. The substrate specifity of enzyme showed a tendency to increase the enzyme activity under addition of dextrin and glycogen, but under saccharose inhibited it. COD removal rate of Aspergillus sp. SN-871 was approximately 67 to 68%.

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