کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8325277 | 1539932 | 2011 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Effect of divalent cations on the porcine kidney cortex membrane-bound form of dipeptidyl peptidase IV
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کلمات کلیدی
BPTISBTIN-ethyl maleimideAPNTLCKAASPNAGIPDPP-IVAPBGLP-1BSA - BSAp-Nitroanilide - p-nitroanilideAlanyl aminopeptidase - آلانیل آمینوپپتیدازbovine serum albumin - آلبومین سرم گاوAminoacids - آمینو اسیدIncretin - افزایشDiabetes - بیماری قندdipeptidyl peptidase IV - دیپپتیدیل پپتیداز IVXaa - زهراZinc - فلز رویtosyl-L-lysine chloromethyl ketone - لسیین کریستالیزل کولینbovine pancreatic trypsin inhibitor - مهار کننده تریپسین پانکراس گاوsoybean trypsin inhibitor - مهارکننده تریپسین سویاNEM - نهglucagon-like peptide 1 - پپتید مشابه گلوکاگون 1Gastric inhibitory peptide - پپتید مهار کننده معدهAPA - چیDivalent cations - کاتیون های دوتاییKidney - کلیهglutamyl aminopeptidase - گلوتامیل آمینوپپتیداز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Effect of divalent cations on the porcine kidney cortex membrane-bound form of dipeptidyl peptidase IV Effect of divalent cations on the porcine kidney cortex membrane-bound form of dipeptidyl peptidase IV](/preview/png/8325277.png)
چکیده انگلیسی
Dipeptidyl peptidase IV is an ectopeptidase with multiple physiological roles including the degradation of incretins, and a target of therapies for type 2 diabetes mellitus. Divalent cations can inhibit its activity, but there has been little effort to understand how they act. The intact membrane-bound form of porcine kidney dipeptidyl peptidase IV was purified by a simple and fast procedure. The purified enzyme hydrolyzed Gly-Pro-p-nitroanilide with an average Vmax of 1.397 ± 0.003 μmol minâ1 mLâ1, kcat of 145.0 ± 1.2 sâ1, KM of 0.138 ± 0.005 mM and kcat/KM of 1050 mMâ1 sâ1. The enzyme was inhibited by bacitracin, tosyl-l-lysine chloromethyl ketone, and by the dipeptidyl peptidase IV family inhibitor l-threo-Ile-thiazolidide (Ki 70 nM). The enzyme was inhibited by the divalent ions Ca2+, Co2+, Cd2+, Hg2+ and Zn2+, following kinetic mechanisms of mixed inhibition, with Ki values of 2.04 Ã 10â1, 2.28 Ã 10â2, 4.21 Ã 10â4, 8.00 Ã 10â5 and 2.95 Ã 10â5 M, respectively. According to bioinformatic tools, Ca2+ ions preferentially bound to the β-propeller domain of the porcine enzyme, while Zn2+ ions to the α-β hydrolase domain; the binding sites were strikingly conserved in the human enzyme and other homologues. The functional characterization indicates that porcine and human homologues have very similar functional properties. Knowledge about the mechanisms of action of divalent cations may facilitate the design of new inhibitors.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 43, Issue 3, March 2011, Pages 363-371
Journal: The International Journal of Biochemistry & Cell Biology - Volume 43, Issue 3, March 2011, Pages 363-371
نویسندگان
Isel Pascual, Hansel Gómez, Tirso Pons, Mae Chappé, Miguel Angel Vargas, Gilberto Valdés, Alà Lopéz, Angélika Saroyán, Jean-Louis Charli, MarÃa de los Angeles Chávez,