http://purl.uniprot.org/citations/16472072 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16472072 | http://www.w3.org/2000/01/rdf-schema#comment | "We studied the processing of amyloid beta-peptides (Abetas) including Abeta(1-40), Abeta(1-42) and pAbeta(3-42) by rat neutral cysteine protease bleomycin hydrolase (BH) according to the methods of SDS-PAGE, HPLC and matrix-assisted laser desorption/inonization time-of-flight mass spectrometry (MALDI-TOF MS). BH significantly processed them by novel features of its diverse activities. It initially cleaved at two sites, His(14)-Gln(15) and Phe(19)-Phe(20) degraded to short intermediates then to amino acids by aminopeptidase and/or carboxypeptidase activities. Also, full-length Abetas were clipped at the carboxyl(C)-terminal region. On the other hand, BH cleaved at only the His(14)-Gln(15) bond in pbetaA(3-42) within a short period of the reaction by endopeptidase activity, and processed the intermediates in order by carboxypeptidase activity. On processing by BH, it found that both fibrillar Abeta(1-40) and Abeta(1-42) were more resistant than non-fibrillar peptides. These results indicate that the processing specificity of BH depends upon the structure and sequence of Abetas."xsd:string |
http://purl.uniprot.org/citations/16472072 | http://purl.org/dc/terms/identifier | "doi:10.2174/092986606775101562"xsd:string |
http://purl.uniprot.org/citations/16472072 | http://purl.uniprot.org/core/author | "Isobe T."xsd:string |
http://purl.uniprot.org/citations/16472072 | http://purl.uniprot.org/core/author | "Kaji H."xsd:string |
http://purl.uniprot.org/citations/16472072 | http://purl.uniprot.org/core/author | "Takeda A."xsd:string |
http://purl.uniprot.org/citations/16472072 | http://purl.uniprot.org/core/author | "Kajiya A."xsd:string |
http://purl.uniprot.org/citations/16472072 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16472072 | http://purl.uniprot.org/core/name | "Protein Pept Lett"xsd:string |
http://purl.uniprot.org/citations/16472072 | http://purl.uniprot.org/core/pages | "119-123"xsd:string |
http://purl.uniprot.org/citations/16472072 | http://purl.uniprot.org/core/title | "Processing of amyloid beta-peptides by neutral cysteine protease bleomycin hydrolase."xsd:string |
http://purl.uniprot.org/citations/16472072 | http://purl.uniprot.org/core/volume | "13"xsd:string |
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