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Titolo:
THE AMINO-ACID-SEQUENCE AND REACTIVE-SITE OF A SINGLE-HEADED TRYPSIN-INHIBITOR FROM WHEAT ENDOSPERM
Autore:
POERIO E; CAPORALE C; CARRANO L; CARUSO C; VACCA F; BUONOCORE V;
Indirizzi:
UNIV TUSCIA,DIPARTIMENTO AGROBIOL & AGROCHIM,VIA S CAMILLO DE LELLIS I-01100 VITERBO ITALY LEPETIT RES CTR GERENZANO ITALY
Titolo Testata:
Journal of protein chemistry
fascicolo: 2, volume: 13, anno: 1994,
pagine: 187 - 194
SICI:
0277-8033(1994)13:2<187:TAAROA>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOWMAN-BIRK TYPE; WATER-SOLUBLE PROTEIN; PURIFICATION; SEEDS; GERM;
Keywords:
TRYPSIN INHIBITOR; WHEAT; PRIMARY STRUCTURE; REACTIVE SITE; BOWMAN-BIRK;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
E. Poerio et al., "THE AMINO-ACID-SEQUENCE AND REACTIVE-SITE OF A SINGLE-HEADED TRYPSIN-INHIBITOR FROM WHEAT ENDOSPERM", Journal of protein chemistry, 13(2), 1994, pp. 187-194

Abstract

The sequence of a trypsin inhibitor, isolated from wheat endosperm, is reported. The primary structure dris obtained by automatic sequence analysis of the S-alkylated protein and of purified peptides derived from chemical cleavage by cyanogen bromide and digestion with Staphylococcus aureus V8 protease. This protein, named wheat trypsin inhibitor (WTI), which is comprised of a total of 71 amino acid residues, has 12cysteines, all involved in disulfide bridges. The primary site of interaction (reactive site) with bovine trypsin has been identified as the dipeptide arginyl-methionyl at positions 19 and 20. WTI has a high degree of sequence identity with a number of serine proteinase inhibitors isolated from both cereal and leguminous plants. On the basis of the findings presented, this protein has been classified as a single-headed trypsin inhibitor of Bowman-Birk type.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 21:01:54