TY - JOUR
T1 - Purification and identification of transglutaminase from mouse coagulating gland and its cross-linking activity among seminal vesicle secretion proteins
AU - Tseng, Huan Chin
AU - Lin, Han Jia
AU - Sudhakar Gandhi, P. S.
AU - Wang, Chia Yih
AU - Chen, Yee Hsiung
N1 - Funding Information:
This work was supported in part by the grants 96-2628-B-001-011-MY2 and 96-3112-B-002-014 from the National Science Council, Taipei, Taiwan. Some of the work described in this paper forms part of a dissertation submitted by HCT in partial fulfillment of the requirement for a Ph.D. at the National Taiwan University.
PY - 2008/12/15
Y1 - 2008/12/15
N2 - 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.
AB - 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.
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U2 - 10.1016/j.jchromb.2008.10.041
DO - 10.1016/j.jchromb.2008.10.041
M3 - Article
C2 - 19027372
AN - SCOPUS:56549088408
SN - 1570-0232
VL - 876
SP - 198
EP - 202
JO - Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
JF - Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
IS - 2
ER -