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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27105

Title: Purification and identification of transglutaminase from mouse coagulating gland and its cross-linking activity among seminal vesicle secretion proteins.
Authors: Huan-Chin Tseng;Han-Jia Lin;P.S. Sudhakar Gandhi;Chia-Yih Wang;Yee-Hsiung Chen
Contributors: NTOU:Institute of Bioscience and Biotechnology
Keywords: Coagulating gland;Protein cross-link;Protein identification;Seminal coagulation;Seminal vesicle;Transglutaminase
Date: 2008-12-15
Issue Date: 2011-10-21T02:22:43Z
Publisher: Journal of Chromatography B
Abstract: Abstract:A 75-kDa protein secreted from mouse coagulating gland was purified to homogeneity by a series of isolation steps including ion exchange chromatography on a DEAE-Sephacel column and ion exchange high-performance liquid chromatography on a sulfopropyl column. It was identified to be Type IV transglutaminase (TG4), based on the establishment of N-terminal sequences by automated Edman degradation together with partial sequences by MS analysis. Its cross-linking activity was tested on the reduced sample of mouse seminal secretion which contained seven major monomer proteins tentatively designated as SVS I–VII. The enzyme was able to cross-link any of SVS I–III but failed to cross-link the other SVS proteins with a Mr value less than 14 kDa. SVS I and SVS III showed comparable substrate activity, but were much weaker than SVS II during the TG4 catalysis.
Relation: 876(2), pp.198–202
URI: http://ntour.ntou.edu.tw/handle/987654321/27105
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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