کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10801036 | 1054724 | 2005 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification, characterization, cDNA cloning, and expression of asialofetuin-binding C-type lectin from eggs of shishamo smelt (Osmerus [Spirinchus] lanceolatus)
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کلمات کلیدی
NTRRTaseabridged universal amplification primerAUAPN-terminal regionRhamnose-binding lectin2-MEHeterodimerRBLGSPPMSFCRDCTRPBSSEFTBSIPTG2-mercaptoethanol - 2-мерکارپتواتانولBSA - BSAGene-specific primer - آغازگر مخصوص ژنbovine serum albumin - آلبومین سرم گاوamino acid - آمینو اسیدAsialofetuin - اسیالفوتینsodium dodecyl sulfate-polyacrylamide gel electrophoresis - الکتروفورز ژل دوده سولفات سدیم پلی آکریل آمیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدisopropyl 1-thio-β-d-galactoside - ایزوپروپیل 1-تیو-ب-د گالاکتوزیدphosphate buffer - بافر فسفاتFish egg - تخم مرغ ماهیReverse transcriptase - ترانس کریپتاز معکوس یا وارونویسrapid amplification of cDNA ends - تقویت سریع cDNA به پایان می رسدcarbohydrate recognition domain - دامنه شناخت کربوهیدراتPhenylmethanesulfonyl fluoride - فنیل متیل سولفونیل فلورایدLuria-Bertani - لواریا بارتانیC-type lectin - لکتین نوع CPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریRace - مسابقهC-terminal region - منطقه C ترمینالhemagglutination unit - واحد هموگلوبین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Purification, characterization, cDNA cloning, and expression of asialofetuin-binding C-type lectin from eggs of shishamo smelt (Osmerus [Spirinchus] lanceolatus) Purification, characterization, cDNA cloning, and expression of asialofetuin-binding C-type lectin from eggs of shishamo smelt (Osmerus [Spirinchus] lanceolatus)](/preview/png/10801036.png)
چکیده انگلیسی
A novel C-type lectin (OLABL) was isolated from the eggs of shishamo smelt [Osmerus (Spirinchus) lanceolatus] by affinity chromatography on asialofetuin-Sepharose. OLABL had a molecular mass of 29 kDa on SDS-PAGE under nonreducing conditions and two subunits with masses of 15 kDa (OLABL-H) and 14 kDa (OLABL-L) under reducing conditions. Thus, OLABL is a heterodimeric protein. cDNA sequence analysis revealed that the H- and L-subunits of OLABL were composed of 137 and 136 amino acid residues, respectively, and showed almost identical (95%) sequences, with slight differences in the N-terminal and C-terminal regions. Since each subunit contained only the characteristic motif of C-type lectin-like domain (CTLD), EPN-E-WND, OLABL is a member of group VII of the CTLD-containing protein family. Although OLABL had an EPN sequence that is known as a mannose-specific motif found in the collectin family, OLABL agglutinated rabbit erythrocytes without the addition of Ca2+ ion, and this activity was inhibited by l-rhamnose and d-galactose derivatives, but not by d-mannose and d-glucose. These results indicate that OLABL has similar characteristics to AJL-2, a calcium-independent lactose specific lectin isolated from Japanese eel skin mucus. Recombinant OLABLs (rHisOLABLs), His-tagged homodimers of the H- and L-subunits, were refolded from inclusion bodies expressed by Escherichia coli. rHisOLABL-L was recovered as a soluble form, but rHisOLABL-H was hardly dissolved in a renaturing buffer. The specific activities of rHisOLABL-L, rHisOLABL-H, and native OLABL were 500, 36, and 20, respectively. These findings suggest that the combination of subunits may affect the solubility and activity of these dimeric form lectins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1725, Issue 2, 15 September 2005, Pages 160-173
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1725, Issue 2, 15 September 2005, Pages 160-173
نویسندگان
Masahiro Hosono, Shigeki Sugawara, Yukiko Ogawa, Takayuki Kohno, Motoaki Takayanagi, Kazuo Nitta,