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Titolo:
LIMITED PROTEOLYSIS OF ALPHA(1)-PROTEINASE INHIBITOR (ALPHA(1)-PL) INACUTE-LEUKEMIA - STUDIES ON THE RESULTING FRAGMENTS AND IMPLICATION FOR THE STRUCTURE OF THE INACTIVATED INHIBITOR
Autore:
DENGLER R; LOTTSPEICH F; OBERTHUR W; MAST AE; EMMERICH B;
Indirizzi:
UNIV MUNICH,KLINIKUM INNENSTADT,MED KLIN,ZIEMSSENSTR 1 D-80336 MUNICHGERMANY MAX PLANCK INST BIOCHEM D-82152 MARTINSRIED GERMANY WASHINGTON UNIV,MED CTR,DIV LAB MED ST LOUIS MO 63130
Titolo Testata:
Biological chemistry Hoppe-Seyler
fascicolo: 3, volume: 376, anno: 1995,
pagine: 165 - 172
SICI:
0177-3593(1995)376:3<165:LPOAI(>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMA ALPHA-1-PROTEINASE INHIBITOR; ANTITHROMBIN-III; ALPHA1-PROTEINASE INHIBITOR; SEC RECEPTOR; ALPHA-1-ANTITRYPSIN; ALPHA-1-ANTICHYMOTRYPSIN; POLYACRYLAMIDE; ANTITRYPSIN; COMPLEXES; PROTEINS;
Keywords:
ACUTE MYELOID LEUKEMIA; ALPHA(1)-PROTEINASE INHIBITOR; LIMITED PROTEOLYSIS; URINARY EXCRETION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
R. Dengler et al., "LIMITED PROTEOLYSIS OF ALPHA(1)-PROTEINASE INHIBITOR (ALPHA(1)-PL) INACUTE-LEUKEMIA - STUDIES ON THE RESULTING FRAGMENTS AND IMPLICATION FOR THE STRUCTURE OF THE INACTIVATED INHIBITOR", Biological chemistry Hoppe-Seyler, 376(3), 1995, pp. 165-172

Abstract

In patients with acute myeloid leukemia, a 41 kDa glycoprotein appears in the urine during remission induction chemotherapy. We have recently reported on the isolation and preliminary characterization of this protein and the generation of specific monoclonal antibodies which showed that it is a proteolytically modified form of alpha(1)-proteinase inhibitor (Dengler at al., 1992, Biol, Chem. Hoppe-Seyler 373, 581-588). In the paper presented here, results from further characterization experiments as well as from studies on the effects of proteolysis on the conformation and the resulting functional properties of the truncated inhibitor are reported, N-terminal amino acid sequence analysis showed that proteolysis has occurred in the N-terminal part as well as inthe reactive site loop of al-PI. The resulting core protein of 41 kDais composed of approximately 324 amino acid residues with the C-terminus located close to Lys(343) of alpha(1)-PI. A4 kDa peptide remainingbound to this fragment throughout the entire purification procedure could be separated by SDS treatment, N- and C-terminal sequence analysis of this peptide after isolation by gel filtration showed that it is comprised of residues Ile(359) up to Lys(394), thus representing the peptide located C-terminal to the reactive site loop of alpha(1)-PI. Transverse urea gradient gel electrophoresis indicates that the proteolyzed inhibitor is in the thermodynamically stable, relaxed (R)-conformation known for proteinase-complexed and cleaved serpins, The truncatedinhibitor exhibits no chemotactic activity towards neutrophils when tested in a standard assay.

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Documento generato il 29/11/20 alle ore 15:46:53