HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Huang, F. Articles by Sasser, R. G. Search for Related Content PubMed PubMed Citation Articles by Huang, F. Articles by Sasser, R. G. Agricola Articles by Huang, F. Articles by Sasser, R. G.

Isolation, Purification, and Characterization of Pregnancy-Specific Protein B from Elk and Moose Placenta¹

^a Department of Animal and Veterinary Science, University of Idaho, Moscow, Idaho 83844 ^b Alaska Department of Fish and Game, Moose Research Center, Soldotna, Alaska 99669 ^c Oregon Department of Fish and Wildlife, La Grande, Oregon 97850

Pregnancy-specific protein B (PSPB) was isolated, purified, and partially characterized from elk and moose placenta. The procedure, which was monitored by bovine PSPB (bPSPB) RIA, included homogenization and extraction in aqueous solution, acidic and ammonium sulfate precipitation, and ion exchange, gel filtration, and affinity chromatographies. The estimated molecular sizes of moose PSPB (mPSPB) were 58 kDa and 31 kDa, and of elk PSPB (ePSPB) were 57 kDa, 45 kDa, and 31 kDa by SDS-PAGE. The isoelectric points of mPSPB were 4.8, 6.6, and 6.7, and of ePSPB were 4.8, 4.9, 6.1, and 6.2 as determined by isoelectric focusing and two-dimensional gel electrophoresis. The carbohydrate contents of mPSPB and ePSPB were approximately 3.15% and 4.98%, respectively. Although ePSPB and mPSPB were recognized by anti-bPSPB in an Ouchterlony double immunodiffusion test, they were found to share identical epitopes and partial identities compared to bPSPB. After treatment at different temperatures (20–60°C) for 1 h, the immunoreactivities of ePSPB and mPSPB in serum were very stable. Only ePSPB in serum treated at 60°C lost some immunoreactivity. After alteration of serum pH (pH 3–11) for 2 h, the immunoreactivities of ePSPB and mPSPB became lower at pH 3 and 4, and remained stable from pH 5 to 11. These data show that moose and elk PSPB have properties similar to those of bovine and ovine PSPB.

¹ This work was supported by The Idaho Agricultural Research Station, Western Regional Research, W112; BioTracking, Moscow, ID; Moose Research Center, Alaska Department of Fish and Game; and the Starkey Project, Oregon Department of Fish and Wildlife.

² Correspondence. FAX: 208 885 6420; gsasser{at}uidaho.edu

This article has been cited by other articles:

				A. L. Hughes, J. A. Green, H. Piontkivska, and R. M. Roberts Aspartic Proteinase Phylogeny and the Origin of Pregnancy-Associated Glycoproteins Mol. Biol. Evol., November 1, 2003; 20(11): 1940 - 1945. [Abstract] [Full Text] [PDF]