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Titolo:
STRUCTURE-FUNCTION STUDIES OF RECOMBINANT MURINE TRIPEPTIDYL-PEPTIDASE-II - THE EXTRA DOMAIN WHICH IS SUBJECT TO ALTERNATIVE SPLICING IS INVOLVED IN COMPLEX-FORMATION
Autore:
TOMKINSON B; HANSEN M; CHEUNG WF;
Indirizzi:
SWEDISH UNIV AGR SCI,CTR BIOMED,DEPT VET MED CHEM,BOX 575 S-75123 UPPSALA SWEDEN UNIV UPPSALA,CTR BIOMED,DEPT MED & PHYSIOL CHEM S-75123 UPPSALA SWEDEN
Titolo Testata:
FEBS letters
fascicolo: 3, volume: 405, anno: 1997,
pagine: 277 - 280
SICI:
0014-5793(1997)405:3<277:SSORMT>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
DYE-BINDING; PROTEIN; CDNA; ENZYME; LIVER; ASSAY; ROLES;
Keywords:
TRIPEPTIDYL-PEPTIDASE II; SERINE PROTEASE; SUBTILISIN TYPE; STRUCTURE-FUNCTION RELATIONSHIP; COMPLEX FORMATION; OLIGOMERIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
19
Recensione:
Indirizzi per estratti:
Citazione:
B. Tomkinson et al., "STRUCTURE-FUNCTION STUDIES OF RECOMBINANT MURINE TRIPEPTIDYL-PEPTIDASE-II - THE EXTRA DOMAIN WHICH IS SUBJECT TO ALTERNATIVE SPLICING IS INVOLVED IN COMPLEX-FORMATION", FEBS letters, 405(3), 1997, pp. 277-280

Abstract

Tripeptidyl-peptidase II (TPP II) is an exopeptidase with a remarkably high native M(r) (>10(6)). Recently, an alternatively spliced, murine cDNA variant was identified which contains an additional 39 bp, encoding 13 amino acids in the C-terminal end of the protein. The two enzyme variants were expressed in human kidney 293 cells. Both types of subunit were found to form the active oligomers. In addition, subunits containing the extra 13 amino acids formed an even larger complex eluting in the void volume of a Sepharose CL-4B column. Thus, it appears that this sequence is important for aggregation of subunits. (C) 1997 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 17:38:01