期刊
BIOLOGICAL CHEMISTRY
卷 391, 期 2-3, 页码 259-270出版社
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2010.016
关键词
aspartic peptidases; cattle; placenta; pregnancy; trophoblast
资金
- Monsanto Co.
- Animal Reproductive Biology Group of the University of Missouri
- Food for the Twenty-first Century Program
- National Institutes of Health [R01 GM57289, GM008396]
The pregnancy-associated glycoproteins (PAGs) represent a complex group of putative aspartic peptidases expressed exclusively in the placentas of species in the Artiodactyla order. The ruminant PAGs segregate into two classes: the 'ancient' and 'modern' PAGs. Some of the modern PAGs possess alterations in the catalytic center that are predicted to preclude their ability to act as peptidases. The ancient ruminant PAGs in contrast are thought to be peptidases, although no proteolytic activity has been described for these members. The aim of the present study was to investigate ( 1) if the ancient bovine PAGs (PAG-2 and PAG-12) have proteolytic activity, and ( 2) if there are any differences in activity between these two closely related members. Recombinant bovine PAG-2 and PAG-12 were expressed in a baculovirus expression system and the purified proteins were analyzed for proteolytic activity against a synthetic fluorescent cathepsin D/E substrate. Both proteins exhibited proteolytic activity with acidic pH optima. The k(cat)/K-m for bovine PAG-2 was 2.7x10(5) M-1 s(-1) and for boPAG-12 it was 6.8x10(4) M-1 s(-1). The enzymes were inhibited by pepstatin A with a K-i of 0.56 and 7.5 nM for boPAG-2 and boPAG-12, respectively. This is the first report describing proteolytic activity in PAGs from ruminant ungulates.
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