نتایج جستجو برای: carbamylation
تعداد نتایج: 238 فیلتر نتایج به سال:
To function, the catalytic sites of Rubisco (EC 4.1.1.39) need to be activated by the reversible carbamylation of a lysine residue within the sites followed by rapid binding of magnesium. The activation of Rubisco in vivo requires the presence of the regulatory protein Rubisco activase. This enzyme is thought to aid the release of sugar phosphate inhibitors from Rubisco's catalytic sites, there...
Abnormal lysyl residues can be detected in aspartate transaminase by following the rate of reaction of amino groups with KN14CO and the rate of enzymatic inactivation. Peptide isolation subsequent to carbamylation of the apoenzyme produces a peptide which is absent in the carbamylated holoenzyme. The composition of the carbamylated peptide matches that of a tryptic peptide containing the active...
Post-translational modifications of proteins significantly affect their structure and function. The carbamylation of positively charged lysine residues to form neutral homoitrulline occurs primarily under inflammatory conditions through myeloperoxidase-dependent cyanate (CNO-) formation. We analyzed the pattern of human IgG1 carbamylation under inflammatory conditions and the effects that this ...
Urea is a normal component of human blood plasma, but it is not inert. Urea-derived cyanate modification of LDL-cholesterol, known as LDL carbamylation, has been discussed for more than a decade. Recent studies have linked LDL carbamylation to atherosclerosis in uraemic patients and animals with chronic kidney disease (CKD). – 4 More broadly, protein carbamylation has been linked with atheroscl...
Cyanate, which is in equilibrium with urea, combines with the alpha-amino group of the aminoterminal valine of hemoglobin in an irreversible, specific carbamylation reaction. Partial carbamylation (0.72 residues/hemoglobin tetramer) as determined by cyanate-(14)C incorporation or hydantoin analysis diminishes the in vitro sickling phenomenon. Since cyanate may react not only with hemoglobin but...
The NH2-terminal valine residues of both chains of oxyhemoglobin S are carbamylated 50 to 100 times faster at pH 7.4 than the a-NH2 groups of the lysine residues of the protein up to a level of 1 carbamyl group per hemoglobin molecule. The pseudo-first order rate constants for the carbamylation of the NHz-terminal residues of carbonmonoxyhemoglobins A and S are identical for the proteins either...
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