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Titolo:
ISOLATION AND CHARACTERIZATION OF GASTRIC TRYPSIN FROM THE MICROSOMALFRACTION OF PORCINE GASTRIC ANTRAL MUCOSA
Autore:
JEOHN GH; SERIZAWA S; IWAMATSU A; TAKAHASHI K;
Indirizzi:
TOKYO UNIV PHARM & LIFE SCI,SCH LIFE SCI,1432-1 HORINOUCHI HACHIOJI TOKYO 19203 JAPAN UNIV TOKYO,FAC SCI,DEPT BIOPHYS & BIOCHEM,BUNKYO KU TOKYO 113 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL YOKOHAMA KANAGAWA 236 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 24, volume: 270, anno: 1995,
pagine: 14748 - 14755
SICI:
0021-9258(1995)270:24<14748:IACOGT>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID SEQUENCE; 4 TANDEM REPEATS; SERINE PROTEASE; PLASMA PREKALLIKREIN; NUCLEOTIDE-SEQUENCE; CDNA; SPECIFICITY; EXPRESSION; INHIBITOR; PANCREAS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
G.H. Jeohn et al., "ISOLATION AND CHARACTERIZATION OF GASTRIC TRYPSIN FROM THE MICROSOMALFRACTION OF PORCINE GASTRIC ANTRAL MUCOSA", The Journal of biological chemistry, 270(24), 1995, pp. 14748-14755

Abstract

A gastric serine protease(s) was found in porcine gastric antral mucosa and was shown to be distributed in the endoplasmic reticulum (ER)-microsome fraction and also in the vesicle fraction. Two forms of the protease were purified over 6,000-fold from the ER-microsome fraction. Analyses of various molecular and enzymatic characteristics including the N-terminal and partial internal amino acid sequences of both formsrevealed that they share the same properties and are indistinguishable from porcine pancreatic trypsin. This is the first time that trypsinor a protease almost identical with trypsin has been found to be present intracellularly in normal tissues. The gastric trypsin activities from the ER-microsome and the vesicle fractions were located in distinct density regions upon density gradient centrifugation, which indicates association of the protease with different organelle membranes. Taken together, these results suggest that there may be a novel function of trypsin in the gastric mucosa; it might function as a specific degrading or processing enzyme as an intracellular protease.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 03:11:40