Purification and identification of transglutaminase from mouse coagulating gland and its cross-linking activity among seminal vesicle secretion proteins

Huan Chin Tseng, Han Jia Lin, P. S. Sudhakar Gandhi, Chia Yih Wang, Yee Hsiung Chen

研究成果: Article同行評審

11 引文 斯高帕斯(Scopus)

摘要

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.

原文English
頁(從 - 到)198-202
頁數5
期刊Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
876
發行號2
DOIs
出版狀態Published - 2008 十二月 15

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Cell Biology

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