کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1216493 | 967017 | 2008 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Purification and identification of transglutaminase from mouse coagulating gland and its cross-linking activity among seminal vesicle secretion proteins Purification and identification of transglutaminase from mouse coagulating gland and its cross-linking activity among seminal vesicle secretion proteins](/preview/png/1216493.png)
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.
Journal: Journal of Chromatography B - Volume 876, Issue 2, 15 December 2008, Pages 198–202