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Titolo:
Serine proteinase inhibitors from eggs and larvae of tick Boophilus microplus: Purification and biochemical characterization
Autore:
Andreotti, R; Malavazi-Piza, KC; Sasaki, SD; Torquato, RJS; Gomes, A; Tanaka, AS;
Indirizzi:
UNIFESP, EPM, Dept Bioquim, BR-04044020 Sao Paulo, Brazil UNIFESP Sao Paulo Brazil BR-04044020 BCim, BR-04044020 Sao Paulo, Brazil Embrapa Gado de Corte, Campo Grande, MS, Brazil Embrapa Gado de Corte Campo Grande MS Brazil e, Campo Grande, MS, Brazil
Titolo Testata:
JOURNAL OF PROTEIN CHEMISTRY
fascicolo: 5, volume: 20, anno: 2001,
pagine: 337 - 343
SICI:
0277-8033(200107)20:5<337:SPIFEA>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
IXODES-DAMMINI; SALIVARY-GLANDS; LYME-DISEASE; AMBLYOMMA-AMERICANUM; ASPARTIC PROTEINASE; CATTLE; ACARI; ANTICOAGULANT; IXODIDAE; EXPRESSION;
Keywords:
serine proteinase inhibitors; Boophilus microplus tick; protein purification; human neutrophil elastase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Tanaka, AS UNIFESP, EPM, Dept Bioquim, BR-04044020 Sao Paulo, Brazil UNIFESP Sao Paulo Brazil BR-04044020 BC4020 Sao Paulo, Brazil
Citazione:
R. Andreotti et al., "Serine proteinase inhibitors from eggs and larvae of tick Boophilus microplus: Purification and biochemical characterization", J PROTEIN C, 20(5), 2001, pp. 337-343

Abstract

The present study describes the purification, characterization, and comparison of serine proteinase inhibitors during the development of egg and larva phases of the tick Boophilus microplus. Samples were collected of eggs between the first day of hatching and the beginning of eclosion (defined as E1, E2, and E3) and of larvae between the first day of eclosion and the infectant phase (defined as L1, L2, and L3). Crude extracts of the samples (2.5% w/v in Tris-HCl buffer) were analyzed by SDS-PAGE, and showed three majorprotein bands of 42, 62, and 85 kDa, differing in intensity, from El to L3samples. The total protein of the larva extracts was 34% less than that ofthe egg extracts, while no differences in active protein were detected. The apparent dissociation constant Ki determined for trypsin was 10-fold lower from E1 to L3 samples. Serine proteinase inhibitors from tick eggs and larvae (BmTls) were purified on trypsin-Sepharose column and analyzed by SDS-PAGE. The results showed a slight difference in protein pattern, with a protein band of 20 kDa in the El and E2 samples which did not appear in the other samples. The K-i for neutrophil elastase was 10-fold lower in L3 than E1. BmTI reverse-phase chromatography showed two and one major peaks in egg and larva samples, respectively. The N-terminal amino acid sequence of the L3 main peak from a C8 column showed a mix of BmTls with the major sequenceAVDFDKGCVPTADPGPCKG. Changes indicated by molecular weight and inhibition activity suggest different roles for BmTIs during the development process.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 01:54:56