کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10235414 | 45036 | 2014 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and partial characterization of a novel hemagglutinating glycoprotein from the cultured mycelia of Hericium erinaceus
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موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
HEG-5, a novel glycoprotein with hemagglutinating activity, was firstly isolated and purified from the cultured mycelia of Hericium erinaceus CZ-2. SDS-PAGE, Native-PAGE and MALDI-TOF-MS proved that HEG-5 was a single band with the molecular weight of approximately 14.4 kDa. HEG-5 had the protein: polysaccharide ratio of approximately 10:1 (%/%) and contained d-glucose, l-rhamnose, d-galactose and d-mannose with a molar ratio of 1.00:1.09:2.45:7.14 in polysaccharide fraction. HEG-5 was an acidic glycoprotein with a PI value of 6.3 and the higher content of acidic amino acids (Asp, 12.42 ± 0.25% and Glu, 12.24 ± 0.26%) in protein fraction. FT-IR and NMR spectra revealed that HEG-5 contained the protein and carbohydrate portions with (1â4)-linked β-galactose residues and β-linked glucose residues. Circular dichroism (CD) demonstrated that HEG-5 was a β-sheet predominant glycoprotein. Hemagglutination assay proved it was a thermo-unstable glycoprotein. The HEG-5 structural novelty was finally presented by protein sequencing and modeling by using MALDI-TOF-MS, NCBI blast search and online SWISS-MODEL Workspace service.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Process Biochemistry - Volume 49, Issue 8, August 2014, Pages 1362-1369
Journal: Process Biochemistry - Volume 49, Issue 8, August 2014, Pages 1362-1369
نویسندگان
Feng-Jie Cui, Yun-Hong Li, Xin-Yi Zan, Yan Yang, Wen-Jing Sun, Jing-Ya Qian, Qiang Zhou, Si-Lian Yu,