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Titolo:
A LYSOSOMAL ARYLAMIDASE IS A MEMBER OF A LARGE FAMILY OF PEPTIDASES IN LYSOSOMES
Autore:
HIROI Y; YAMAMOTO S; OKA T;
Indirizzi:
NAKAMURA GAKUEN UNIV,DEPT NUTR CHEM,JONAN KU FUKUOKA 814 JAPAN UNIV RYUKYUS,SCH HLTH SCI UEHARA OKINAWA 90301 JAPAN UNIV RYUKYUS,COMPREHENS MED RES CTR UEHARA OKINAWA 90301 JAPAN UNIV TOKUSHIMA,SCH MED,DEPT NUTR CHEM TOKUSHIMA 770 JAPAN
Titolo Testata:
Biochemistry and molecular biology international
fascicolo: 4, volume: 34, anno: 1994,
pagine: 713 - 721
SICI:
1039-9712(1994)34:4<713:ALAIAM>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
MONKEY BRAIN; RAT-LIVER; AMINOPEPTIDASE; PURIFICATION; ENKEPHALIN; HYDROLYSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
Y. Hiroi et al., "A LYSOSOMAL ARYLAMIDASE IS A MEMBER OF A LARGE FAMILY OF PEPTIDASES IN LYSOSOMES", Biochemistry and molecular biology international, 34(4), 1994, pp. 713-721

Abstract

One form (form VI) of lysosomal arylamidase, having a molecular weight of 135,000 and an isoelectric point of 7.8, was purified from rat liver to apparent electrophoretic homogeneity. The enzyme consisted of three identical polypeptides with a molecular weight of 45,000, as judged by disk electrophoresis in the presence of sodium dodecyl sulfate (SDS). The enzyme hydrolyzed di- and tripeptides. The enzyme released aN-terminal amino acid from Leu(5)-enkephalin and Met-Lys-bradykinin; these have a tyrosine and a methionine at the N-terminus, respectively. The enzyme did not hydrolyze bradykinin, angiotensin and melanocyte-stimulating hormone release-inhibitory factor (MIF); these have a basic amino acid, an acidic amino acid, and a proline at the N-terminus, respectively.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:38:29