Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
CRY-J-I, A MAJOR ALLERGEN OF JAPANESE CEDAR POLLEN, HAS PECTATE LYASEENZYME-ACTIVITY
Autore:
TANIGUCHI Y; ONO A; SAWATANI M; NANBA M; KOHNO K; USUI H; KURIMOTO M; MATUHASI T;
Indirizzi:
HAYASHIBARA BIOCHEM LABS INC,FUJISAKI INST,675-1 FUJISAKI OKAYAMA 702JAPAN OKINAKA MEM INST MED RES TORANOMON 105 JAPAN
Titolo Testata:
Allergy
fascicolo: 1, volume: 50, anno: 1995,
pagine: 90 - 93
SICI:
0105-4538(1995)50:1<90:CAMAOJ>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYPTOMERIA-JAPONICA POLLEN; ERWINIA-CHRYSANTHEMI EC16; SUGI BASIC-PROTEIN; MONOCLONAL-ANTIBODIES; ANTIGENIC ANALYSES; ESCHERICHIA-COLI; EXPRESSION; GENES; EPITOPES; SEQUENCE;
Keywords:
CRY J I; JAPANESE CEDAR POLLEN; PECTATE LYASE; POLLINOSIS;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
Y. Taniguchi et al., "CRY-J-I, A MAJOR ALLERGEN OF JAPANESE CEDAR POLLEN, HAS PECTATE LYASEENZYME-ACTIVITY", Allergy, 50(1), 1995, pp. 90-93

Abstract

In the course of analyzing the partial amino acid sequences of Cry j I, a major allergen of Japanese cedar (Cryptomeria japonica) pollen, we found a peptide fragment which has a significant homology to some pectate lyase isozymes secreted by plant pathogenic bacteria. Therefore,we investigated whether Cry j I has pectate lyase activity. Cry j I reacted with polygalacturonic acid, resulting in the release of unsaturated uronide products. The optimum temperature and pH for the reactionwere 60-70 degrees C and pH 10. The enzymatic reaction had an absolute Ca2+ ion requirement. These characteristics were very compatible with the character of the pectate lyase isozymes reported previously. These results clearly show that Cry j I has pectate lyase activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 02:28:38