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Titolo:
PURIFICATION, CHARACTERIZATION, AND CDNA CLONING OF A KUNITZ-TYPE PROTEINASE-INHIBITOR SECRETED BY THE PORCINE UTERUS
Autore:
STALLINGSMANN ML; BURKE MG; TROUT WE; ROBERTS RM;
Indirizzi:
UNIV MISSOURI,AMIM SCI RES CTR 158,DEPT ANIM SCI COLUMBIA MO 65211 UNIV MISSOURI,AMIM SCI RES CTR 158,DEPT ANIM SCI COLUMBIA MO 65211 UNIV MISSOURI,DEPT BIOCHEM COLUMBIA MO 65211
Titolo Testata:
The Journal of biological chemistry
fascicolo: 39, volume: 269, anno: 1994,
pagine: 24090 - 24094
SICI:
0021-9258(1994)269:39<24090:PCACCO>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
PANCREATIC TRYPSIN-INHIBITOR; PLASMINOGEN-ACTIVATOR PRODUCTION; RETINOL-BINDING PROTEIN; MOLECULAR-CLONING; CRYSTAL-STRUCTURE; PIG TROPHOBLAST; MESSENGER-RNA; EXPRESSION; PREGNANCY; IMPLANTATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
M.L. Stallingsmann et al., "PURIFICATION, CHARACTERIZATION, AND CDNA CLONING OF A KUNITZ-TYPE PROTEINASE-INHIBITOR SECRETED BY THE PORCINE UTERUS", The Journal of biological chemistry, 269(39), 1994, pp. 24090-24094

Abstract

The porcine uterus synthesizes a proteinase inhibitor (M(r) 14,000) under the influence of progesterone that is relatively specific for plasmin and trypsin, but that also has weak affinity for chymotrypsin. Several isoforms of this uterine plasmin/trypsin inhibitor were purifiedby a procedure whose final two steps involved affinity chromatographyon immobilized chymotrypsin and cation exchange chromatography. Amino-terminal sequencing showed that at least three of the isoforms were closely related. An oligonucleotide probe based on the protein sequencewas used to identify a cDNA that contained an open reading frame coding for a mature protein (M(r) 10,295) of 98 amino acids. The inhibitorhad a well defined, but unique, Kunitz domain of 64 residues at its amino terminus that shared 67% sequence identity to bovine pancreatic trypsin inhibitor. Its P-1 residue was arginine rather than lysine. Northern analysis showed the presence of a single mRNA species (700 bases) that in adult female pigs appeared to be confined to the uterus. During pregnancy, UPTI mRNA expression was high until Day 30 and decreased significantly thereafter. By contrast, uteroferrin mRNA reached maximal concentrations in late pregnancy. These data are consistent with an earlier hypothesis that the inhibitor serves to neutralize the activities of one or more serine proteinases generated by the proliferatingtrophoblast during the formation of the noninvasive placenta of the pig.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 16:46:55