Biochemical characterization of recombinant Penaeus vannamei trypsinogen.
Comp Biochem Physiol B Biochem Mol Biol
; 238: 110337, 2019 Dec.
Article
em En
| MEDLINE
| ID: mdl-31476362
ABSTRACT
Trypsinogens are the inactive precursors of trypsins (EC 3.4.21.4), which are digestive serine proteases. Despite knowing the properties of trypsins from Pacific white shrimp, Penaeus vannamei, the biochemical properties of shrimp trypsinogens including activation mechanisms and kinetics are unknown, due to difficulties isolating them from natural sources. In the present work, we describe the purification and biochemical characterization of four trypsinogen-like isoforms from recombinant P. vannamei trypsinogen, with a special emphasis on understanding its activation kinetics. The major trypsinogen-like isoform had an apparent molecular mass of 29â¯kDa. The other three forms of recombinant trypsinogen were an N-glycosylated form of 32â¯kDa, a possibly O-glycosylated form of 41â¯kDa, and a likely double-chain form with a subunit of 23â¯kDa. The autoactivation profile of three-recombinant trypsinogen-like isoforms showed increased trypsin activity at a rate that was higher than that of bovine trypsinogen. This confirms the hypothesis proposed in the literature of a rapid trypsinogen autoactivation in the absence of aspartates in the activation peptide as it is for P. vannamei trypsinogen.
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Base de dados:
MEDLINE
Assunto principal:
Tripsinogênio
/
Penaeidae
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Proteínas de Artrópodes
Limite:
Animals
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article