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10.1016/s0014-5793(02)03513-5 http://scihub22266oqcxt.onion/10.1016/s0014-5793(02)03513-5 12417322!ä!12417322 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       FEBS+Lett 2002 ; 531 (2): 255-8 Nephropedia Template TP {{tp|p=12417322|t=2002. Identification of the amino terminal subunit of the glycoprotein of Borna disease virus |pdf=|usr=}}{{12417322}} gab.com Text Identification of the amino terminal subunit of the glycoprotein of Borna disease virus JO: FEBS Lett http://www.kidney.de/pget.php?&tw=1&pmid=12417322 #FOAvip The only surface membrane glycoprotein of Borna disease virus (BDV) is synthesized as a polypeptide with a molecular mass of 57 kDa and N-glycosylated to a precursor glycoprotein (GP) of about 94 kDa. It is processed by the cellular protease furin into the C-terminal membrane-anchored subunit GP-C, also known as gp43, and a presumptive N-terminal subunit GP-N, that is highly glycosylated and has a molecular mass of about 51 kDa. However, up to now the latter remained undetected in BDV-infected material. We describe a novel approach to identify glycan masked linear antigenic epitopes. In the present study, GP-N was identified in BDV-infected cells by a combination of lectin precipitation, enzymatic deglycosylation on blot and immunochemistry using an N-terminal specific antiserum. The GP-N has an apparent molecular mass of 45-50 kDa in its glycosylated form and 27 kDa in its deglycosylated form. N-glycan analysis revealed that the precursor GP contains only mannose-rich N-glycans, whereas GP-N and GP-C contain mannose-rich and complex-type N-glycans. Twit Text FOAVip Identification of the amino terminal subunit of the glycoprotein of Borna disease virus ????FEBS Lett http://www.kidney.de/pget.php?&tw=1&pmid=12417322 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=12417322 #FOAvip English Wikipedia <ref>{{Cite pmid|12417322}}</ref> Identification of the amino terminal subunit of the glycoprotein of Borna disease virus #MMPMID12417322 Kiermayer S; Kraus I; Richt JA; Garten W; Eickmann M FEBS Lett 2002[Nov]; 531 (2): 255-8 PMID12417322show ga The only surface membrane glycoprotein of Borna disease virus (BDV) is synthesized as a polypeptide with a molecular mass of 57 kDa and N-glycosylated to a precursor glycoprotein (GP) of about 94 kDa. It is processed by the cellular protease furin into the C-terminal membrane-anchored subunit GP-C, also known as gp43, and a presumptive N-terminal subunit GP-N, that is highly glycosylated and has a molecular mass of about 51 kDa. However, up to now the latter remained undetected in BDV-infected material. We describe a novel approach to identify glycan masked linear antigenic epitopes. In the present study, GP-N was identified in BDV-infected cells by a combination of lectin precipitation, enzymatic deglycosylation on blot and immunochemistry using an N-terminal specific antiserum. The GP-N has an apparent molecular mass of 45-50 kDa in its glycosylated form and 27 kDa in its deglycosylated form. N-glycan analysis revealed that the precursor GP contains only mannose-rich N-glycans, whereas GP-N and GP-C contain mannose-rich and complex-type N-glycans. |*Borna disease virus/immunology[MESH] |Animals[MESH] |Cell Line[MESH] |Chlorocebus aethiops[MESH] |Dogs[MESH] |Glycoproteins/analysis/*chemistry/immunology[MESH] |Glycoside Hydrolases[MESH] |Immunoblotting[MESH] |Lectins/metabolism[MESH] |Mannose/analysis[MESH] |Molecular Weight[MESH] |Polysaccharides/chemistry[MESH] |Protein Subunits[MESH] |Vero Cells[MESH]Identification of the amino terminal subunit of the glycoprotein of Bo(epmc).pdf DeepDyve Pubget Overpricing