Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/25395
Title: STRUCTURAL REQUIREMENTS of BIOACTIVE PEPTIDES for INTERACTION WITH ENDOPEPTIDASE-22.19
Authors: Camargo, ACM
Gomes, M. D.
Toffoletto, O.
Ribeiro, MJF
Ferro, E. S.
Fernandes, B. L.
Suzuki, K.
Sasaki, Y.
Juliano, L.
Universidade de São Paulo (USP)
TOKOHU COLL PHARM
Universidade Federal de São Paulo (UNIFESP)
Issue Date: 1-Apr-1994
Publisher: Churchill Livingstone
Citation: Neuropeptides. Edinburgh: Churchill Livingstone, v. 26, n. 4, p. 281-287, 1994.
Abstract: A series of biologically active peptides and related compounds (opioid peptides, neurotensin, and bradykinin) were used as substrates or competitive inhibitors to study the structural requirements for peptide interaction with endopeptidase 22.19. the kinetics of hydrolysis of these peptides indicated that, in contrast to other proteases, the substrate specificity of endopeptidase 22.19 is not determined by the amino acids flanking the sensitive bonds of the substrates. the competition between bioactive peptide analogues and the quenched fluorescence substrate of endopeptidase 22.19 indicated that their length and their flexibility may be the dominant factors to explain their binding specificities. These peculiar features of endopeptidase 22.19 may be of importance to understand the physiological processes of conversion and inactivation of biologically active peptides.
URI: http://repositorio.unifesp.br/handle/11600/25395
ISSN: 0143-4179
Other Identifiers: http://dx.doi.org/10.1016/0143-4179(94)90083-3
Appears in Collections:Em verificação - Geral

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