Hydrolysis of somatostatin by human tissue kallikrein after the amino acid pair Phe-Phe

Hydrolysis of somatostatin by human tissue kallikrein after the amino acid pair Phe-Phe

Author Pimenta, Daniel Carvalho Autor UNIFESP Google Scholar
Juliano, Maria Aparecida Autor UNIFESP Google Scholar
Juliano, Luiz Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Abstract Somatostatin-(1-14) was hydrolysed by human tissue kallikrein at the Phe(7)-Trp(8) bond, after a Phe-Phe pair of amino acids, with similar kinetic parameters to those described for human high- and low-molecular-mass kininogens. Substance P and human insulin, which also contain a Phe-Phe pair in their sequences, were both resistant. More details of this hydrolytic specificity of human tissue kallikrein were obtained by synthesizing and assaying internally quenched fluorescent peptides containing the sequence of somatostatin-(1-14), as well as the reactive-centre loop of human kallikrein-binding protein (kallistatin). We also observed that human tissue kallikrein hydrolysed growth hormone-releasing hormone at the Arg(11)-Lys(12) bond, although this peptide contains in its structure a pair of leucines (Leu(22)-Leu(23)), in contrast with the Phe-Phe pair in somatostatin. We have also demonstrated the susceptibility to human tissue kallikrein of some chromogenic peptides with the general structure X-Phe-Phe-p-nitroanilide and of D-Pro-Phe-Phe-4-methylcoumaryl-7-amide.
Language English
Date 1997-10-01
Published in Biochemical Journal. London: Portland Press, v. 327, n. 1, p. 27-30, 1997.
ISSN 0264-6021 (Sherpa/Romeo, impact factor)
Publisher Portland Press
Extent 27-30
Origin http://dx.doi.org/10.1042/bj3270027
Access rights Open access Open Access
Type Article
Web of Science ID WOS:A1997XZ16200004
URI http://repositorio.unifesp.br/11600/42802

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