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

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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.

Original languageEnglish
Pages (from-to)198-202
Number of pages5
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume876
Issue number2
DOIs
Publication statusPublished - 2008 Dec 15

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All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Cell Biology

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