[Evaluation of respiratory parameters in patients with chronic obstructive lung disease during physical exercises].

Aim: To study the relationship between the indicators of dynamic capnography and pulse oximetry with the indicators of the 6-minute walk test (6MWT) in patients with chronic obstructive pulmonary disease (COPD).

Materials And Methods: 67 patients of both sexes were examined: 45 patients with COPD (age 60.02.

Study of interaction of ceruloplasmin with serprocidins.

This paper describes formation of complexes of ceruloplasmin (CP) with such proteins of the serprocidin family as azurocidin (CAP37), neutrophilic elastase (NE), cathepsin G (CG), and proteinase 3 (PR3). We present evidence that serprocidins form complexes with CP at a molar ratio 1 : 1. Phenylmethylsulfonyl fluoride, a serine protease inhibitor, did not prevent the interaction of serprocidins with CP in the course of SDS-free disc electrophoresis.

Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin.

The first evidence of multi-component complexes formed by myeloperoxidase (MPO), ceruloplasmin (CP), and very low/low density lipoproteins (VLDL/LDL) obtained by electrophoresis, gel filtration, and photon-correlation spectroscopy (PCS) is presented in this paper. Complexes were observed when isolated MPO, CP, and VLDL/LDL were mixed and/or when MPO was added to the blood plasma. Complex LDL-MPO-CP was detected in 44 of 100 plasma samples taken from patients with atherosclerosis, and 33 of 44 samples also contained the VLDL-MPO-CP complex.

Identification of complexes formed by ceruloplasmin with matrix metalloproteinases 2 and 12.

Marked sensitivity to proteolytic degradation results in the loss of multiple antioxidant properties of ceruloplasmin (CP), the multicopper oxidase of mammalian plasma. In this study, gel filtration of virtually pure CP (purity 99.7%) yielded complexes of this protein.

Effect of lactoferrin on oxidative features of ceruloplasmin.

In our previous report we first described a complex between lactoferrin (Lf) and ceruloplasmin (Cp) with K (d) approximately 1.8 microM. The presence of this complex in colostrum that never contains more than 0.

Ceruloplasmin and myeloperoxidase in complex affect the enzymatic properties of each other.

Ceruloplasmin (CP), the multicopper oxidase of plasma, interacts with myeloperoxidase (MPO), an enzyme of leukocytes, and inhibits its peroxidase and chlorinating activity. Studies on the enzymatic properties shows that CP behaves as a competitive inhibitor impeding the binding of aromatic substrates to the active centre of MPO. The contact between CP and MPO probably entails conformational changes close to the p-phenylenediamine binding site in CP, which explains the observed activation by MPO of the substrate's oxidation.

[A study of the effect of ceruloplasmin and lactoferrin on the chlorination activity of leukocytic myeloperoxidase using the chemiluminescence method].

The chlorination activity of free myeloperoxidase and myeloperoxidase bound with ceruloplasmin or with both ceruloplasmin and lactoferrin has been studied by luminal-dependent chemiluminescence. It was shown that the addition of hydrogen peroxide to the "myeloperoxidase + Cl- + luminal" system is accompanied by a fast flash of light emission. In the absence of myeloperoxidase or Cl-, the flash intensity was considerably reduced.

Identification of leukocyte cationic proteins that interact with ceruloplasmin.

Proteins from leukocytes were investigated for their ability to interact with ceruloplasmin (Cp), a copper-containing glycoprotein of human plasma. Extract from leukocytes was subjected to affinity chromatography on Cp-Sepharose, after which proteins were eluted from the resin with 0.5 M NaCl in Tris-HCl, pH 7.

Interaction of ceruloplasmin, lactoferrin, and myeloperoxidase.

When lactoferrin (LF) and myeloperoxidase (MPO) are added to ceruloplasmin (CP), a CP-LF-MPO triple complex forms. The complex is formed under physiological conditions, but also in the course of SDS-free PAGE. Polyclonal antibodies to both LF and MPO displace the respective proteins from the CP-LF-MPO complex.