Purification and identification of transglutaminase from mouse coagulating gland and its cross-linking activity among seminal vesicle secretion proteins
Resource
Journal of Chromatography B 876 (2): 198-202
Journal
Journal of Chromatography B
Pages
198-202
Date Issued
2008
Date
2008
Author(s)
Tseng, Huan-Chin
Lin, Han-Jia
Sudhakar Gandhi, P.S.
Wang, Chia-Yih
Chen, Yee-Hsiung
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 (TG(4)), 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 M(r) value less than 14 kDa. SVS I and SVS III showed comparable substrate activity, but were much weaker than SVS II during the TG(4) catalysis.
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