کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9442974 | 1302612 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A novel protease from Entamoeba histolytica homologous to members of the family S28 of serine proteases
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
TPCKdi-isopropyl fluorophosphatePRCPSBTIN-tosyl-l-phenylalanine chloromethyl ketoneTLCK2D-PAGEDPPE-64PMSFDFPEntamoeba histolytica - Entamoeba هیستولیتیکاEDTA - اتیلن دی آمین تترا استیک اسید Ethylenediaminetetraacetic acid - اتیلینیدامین تتراستیک اسیدtwo-dimensional polyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمید دو بعدیdipeptidyl peptidase - دیپپتیدیل پپتیدازSerine protease - سرین پروتئازphenylmethylsulfonyl fluoride - فنیل متیل سولفونیل فلورایدsoybean trypsin inhibitor - مهارکننده تریپسین سویاProlylcarboxypeptidase - پرولیارکسی سایپتیداز
موضوعات مرتبط
علوم زیستی و بیوفناوری
ایمنی شناسی و میکروب شناسی
انگل شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: A novel protease from Entamoeba histolytica homologous to members of the family S28 of serine proteases A novel protease from Entamoeba histolytica homologous to members of the family S28 of serine proteases](/preview/png/9442974.png)
چکیده انگلیسی
Serine proteases are one of the biologically most important and widely distributed enzyme families. A protease capable of degrading the substrate Suc-AAF-AMC was isolated from axenically grown trophozoites of Entamoeba histolytica. The enzyme was purified by ion-exchange chromatography and electroelution, and appeared on 2D-PAGE as a spot of 60 kDa and pI of 4.65. Data obtained from zymogram suggest the active protease is present either as homodimer (130 kDa) or homotetramer (250 kDa). The optimal temperature of the enzyme was 37 °C, and it exhibited activity over a broad pH range. The protease was strongly inhibited by TPCK and chelating agents. The enzymatic activity was restored upon addition of calcium. BLAST analysis with the sequence of internal peptides of the protein revealed two open reading frames within the genome of E. histolytica, homologous to members of the family S28, clan SC of serine proteases.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Parasitology - Volume 110, Issue 3, July 2005, Pages 270-275
Journal: Experimental Parasitology - Volume 110, Issue 3, July 2005, Pages 270-275
نویسندگان
Minerva Paola Barrios-Ceballos, Norma Angélica MartÃnez-Gallardo, Fernando Anaya-Velázquez, David Mirelman, Felipe Padilla-Vaca,