Expression, purification, and characterization of the Kunitz-type proteinase inhibitor domain of the amyloid [beta]-protein precursor-like protein-2
dc.contributor.author | Van Nostrand, William E. | en_US |
dc.contributor.author | Schmaier, Alvin H. | en_US |
dc.contributor.author | Neiditch, Barry R. | en_US |
dc.contributor.author | Siegel, Robert S. | en_US |
dc.contributor.author | Raschke, William C. | en_US |
dc.contributor.author | Sisodia, Sangram S. | en_US |
dc.contributor.author | Wagner, Steven L. | en_US |
dc.date.accessioned | 2006-04-10T17:42:21Z | |
dc.date.available | 2006-04-10T17:42:21Z | |
dc.date.issued | 1994-12-14 | en_US |
dc.identifier.citation | Van Nostrand, William E., Schmaier, Alvin H., Neiditch, Barry R., Siegel, Robert S., Raschke, William C., Sisodia, Sangram S., Wagner, Steven L. (1994/12/14)."Expression, purification, and characterization of the Kunitz-type proteinase inhibitor domain of the amyloid [beta]-protein precursor-like protein-2." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1209(2): 165-170. <http://hdl.handle.net/2027.42/31134> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T21-47PYGTR-2/2/97e5fcbb114db2f2e9ee68c9d89b84ef | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/31134 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=7811686&dopt=citation | en_US |
dc.description.abstract | In this report we describe the use of the methylotrophic industrial yeast Pichia pastoris as a host system for the large scale production of the Kunitz-type proteinase inhibitor (KPI) domain of the amyloid [beta]-protein precursor-like protein-2 (APLP-2). The expression plasmid for the KPI domain of APLP-2 encoded amino acids 305-364 of the APLP-2 cDNA (Slunt et al. (1994) J. Biol. Chem. 269, 2637-2644). The secreted 60 amino-acid product was purified to homogeneity and biochemically characterized. Amino-acid sequencing of the expressed KPI domain of APLP-2 verified its integrity. The proteinase inhibitory properties of the KPI domain of APLP-2 were compared to those of the KPI domain of proteinase nexin-2/amyloid [beta]-protein precursor (PN-2/A[beta]PP). Both KPI domains potently inhibited trypsin and, to a lesser extent, chymotrypsin, plasmin, and coagulation factors XIa and IXa. However, the KPI domain of APLP-2 was a [approximate]20-fold less effective inhibitor of coagulation factor XIa compared to the KPI domain of PN-2/A[beta]PP. Similarly, the KPI domain of APLP-2 was a less effective anticoagulant in coagulation based assays than the KPI domain of PN-2/A[beta]PP. These studies indicate that the KPI domains of PN-2/A[beta]PP and APLP-2 form a family of proteinase inhibitors although the former is a better inhibitor of factor XIa and a more potent anticoagulant than the latter. | en_US |
dc.format.extent | 495519 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Expression, purification, and characterization of the Kunitz-type proteinase inhibitor domain of the amyloid [beta]-protein precursor-like protein-2 | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Internal Medicine, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationother | Department of Microbiology and Molecular Genetics, College of Medicine, University of California, Irvine, CA 92717-4025, USA | en_US |
dc.contributor.affiliationother | Salk Institute Biotechnology/Industrial Associates, 505 Coast Blvd. South, La Jolla, CA, USA | en_US |
dc.contributor.affiliationother | Salk Institute Biotechnology/Industrial Associates, 505 Coast Blvd. South, La Jolla, CA, USA | en_US |
dc.contributor.affiliationother | Salk Institute Biotechnology/Industrial Associates, 505 Coast Blvd. South, La Jolla, CA, USA | en_US |
dc.contributor.affiliationother | Department of Pathology, The Johns Hopkins University School of Medicine, Baltimore, MD, USA | en_US |
dc.contributor.affiliationother | Salk Institute Biotechnology/Industrial Associates, 505 Coast Blvd. South, La Jolla, CA, USA | en_US |
dc.identifier.pmid | 7811686 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/31134/1/0000031.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0167-4838(94)90180-5 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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