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Nmr studies of human cystatin C - stable isotope labeling of human cystatin C

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Jurczak P. , Maszota-Zieleniak M.

tom Vol. 18, No 4

327--330

The objective of this study was to obtain a double and triple labeled hu man cystatin C (h CC ). Another objective was to record sets of 2D and 3D NMR spectra of the h CC dimer (in a solution) using a 700MHz spectrometer. The data obtained durin g attempts to determine the NMR structure should provide useful information about chemical shifts of amino acid residues. They will certainly accelerate solving the human cys tatin C NMR structure. In this paper the main focus is put on triple isotopic labeling, protein overproduction and NMR analysis of h CC . The first two processes lead to obtaining h CC labeled with stable isotopes of carbon ( 13 C), nitrogen ( 15 N) and hydrogen ( 2 H) (double labeled h CC was obtained with a similar method). The obtained protein was later used for the purp ose of NMR spectra.

Partial hypoxanthine - guanine phosphoribosyltransferase deficiency in young man

100%

Kumsta M. , Krijt J. , Sebesta I.

nr 3

Overproduction and purification of the CepA protein from Lactococcus lactis

100%

Kowalczyk M. , Bardowski J.

nr 2

In this work we present cloning and overexpression of lactococcal CcpA protein in Escherichia coli Xllblue strain as a fusion with 6xHis tag. A high yield of the CcpA protein was obtained when the cells were cultured in liquid medium LB with 100 ug/ml ampicillin at 37°C and subsequently for 4 h after induction by IPTG. The procedure let us obtain 5 mg of homogenous CcpA protein. Glutaraldehyde crosslinking analysis indicated the formation of dimer or tetramer forms of the CcpA protein.