Sinisa Ubovic Knjiga Pdf Download

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Sinisa Ubovic Knjiga Pdf Download

cystatin-C.
cystatin-C is a natural inhibitor of cathepsins S and L (cysteine proteinases) because they target cystatin-C for the lysosome.
The C-terminal peptide sequence of cystatin-C corresponding to the cleavage site at residue 69 of natural human cystatin-C, contains the LPYSK motif which is necessary for binding cystatin-C in the lysosome. The mutated form of cystatin-C C69A, resistant to cathepsin S and L, is unable to inhibit cathepsins S and L, being rather a substrate of these proteinases, similar to other cystatins.
If the cystatin-C C69A is endocytosed by a cell, it does not get into the lysosome, and cannot inhibit cysteine proteinases. Thus, although this cystatin-C form is not destroyed by proteases, it nevertheless cannot inhibit these enzymes.
. Christiana Quintay. A single-electrode B1Bx generator has been used to monitor the cardiac activity and serum concentrations of cystatin C in eighteen patients with acute myocardial infarction undergoing thrombolytic therapy.
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Back to Terms and ConditionsAnalysis of stereoselectivity of siRNAs: development of a MALDI-TOF mass spectrometry method.
RNA interference (RNAi) is a well-described post-transcriptional gene silencing phenomenon that has immense potential for use in the study of gene function. Many synthetic siRNAs have been developed for use in functional studies. Here we describe an analysis of the stereochemistry of siRNAs using a simple mass spectrometry method. The introduction of 2′-O-methyl groups at 2 and 8 positions of the siRNA backbone has been shown to facilitate efficient and site-specific coupling of a 5′-amino group to the 2′-O-Me-RNA with the help of 2′,3′-O,O’-cycl

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