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Mediators of Inflammation
Volume 13, Issue 4, Pages 263-268
http://dx.doi.org/10.1080/09629350400003068

Effects of 'casoparan', a peptide isolated from casein hydrolysates with mastoparan-like properties

1Biochemistry and Biophysics Laboratory, Butantan Institute, São Paulo, Brazil
2Biophysics Department, UNIFESP, São Paulo, Brazil
3Physiopathology Laboratory, Butantan Institute, São Paulo, Brazil

Copyright © 2004 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

CASEIN, a protein found in milk of several species, is divided into different chains from 19 to 25 kDa. Casein is also considered as a source of amino acids and generating peptides with biological activities such as opiate, immunostimulating, antibacterial, peptidase inhibitors, among others.

In this work, Sephadex G-10 chromatography followed by high-performance liquid chromatography isolation purified NZCase TT, an industrial culture media for tetanus toxin production. In the first step, four pools were isolated and tested in different assays: isolated smooth muscle assay (guinea pig ileum, rat uterus), phagocytosis in vitro of opsonized sheep red blood cells, and hydrogen peroxide (H2O2) release from mouse peritoneal macrophages.

Pool III was the main active pool being able to potentiate bradykinin action in guinea pig ileum, stimulating phagocitic activity by resident macrophages and increasing H2O2 release from macrophages previously activated with bacille Calmette Guérin.

Using mass spectra the primary structure of the main peptide from pool III was obtained – INKKI, which corresponds to β-casein fragment 26-30.

The immunostimulating action is probably related to a direct action in macrophage cells.