Competitive inhibition of adenosine deaminase by urea, guanidine, biuret, and guanylurea.
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Biomedical subjects
Publications and source records attributed to G Ronca.
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A study has been carried out on the formation of -SH groups and of cysteine and cystine from 4-carbomethoxythiazolidin HCl through human expectorate mucus and lung homogenates. Both the expectorate and the homogenate, revealed to be able to metabolize TCM to cysteine releasing free -SH groups. The speed of cysteine formation is higher for the homogenate, but also the expectorate revealed to be very effective for the metabolization to cysteine. Furthermore it has been demonstrated that the TCM, incubated with human expectorate in presence and in absence of lung homogenate, can modify the chemical-physical characteristics of the mucus, rendering it more soluble and less viscous, i.e. displaying a mucolytic activity. These results account for the in-vitro experimental base to the observation that the product has a mucolytic activity whether administered by os or by aerosol.
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Circular dichroism studies with adenosine deaminase from calf intestinal mucosa are described. Addition of purine riboside, a competitive inhibitor of the enzyme, does not cause modification of mean residue ellipticity in the CD spectra in the region between 250 and 185 nm, but increases markedly the ellipticity in the 300-250 nm region. The data are consistent with the view that a conformational change involving aromatic amino acid residues occurs upon binding of purine riboside to adenosine binding site of adenosine deaminase.
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