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“By way of hydrogen bonding, the arginine sidechain orients the histidine of the catalytic dyad in an orientation that is favorable for proteolysis (Fig. 2).”
Journal of biomedical nanotechnology • 2015 | View Paper
“Addition of histidines imparts endosomal escape property to arginine homopeptide, but their arrangement with respect to arginines is more critical in controlling DNA condensation, release and transfection efficiency.”
“Substitution of an arginine at position 433 with a histidine [TNSALP(R433H)] or a cysteine [TNSALP(R433C)] was reported in patients diagnosed with the mild or severe form of hypophosphatasia, respectively.”
“It is noteworthy that an important role of arginine was identified for regulating agonist-mediated internalization when a histidine (R149H) was present.”
“Amino acid metabolism was stimulated in tumor-bearing animals after receiving 4 or 6% arginine , demonstrated by significant increase of arginine, ornithine, citrulline, proline and histidine levels in the blood (p ≤ 0.001) when compared to the control diet group.”
Annals of Nutrition and Metabolism • 2004 | View Paper
“… arginine … histidine residue resulted in 13.7% residual enzyme activity, with an apparent K(m) value (133 microM) lower than that found for the normal enzyme (… arginine with proline resulted in total absence of residual activity, in agreement with the phenotypes observed in patients carrying R88H and R88P mutations.”
“Single replacement of histidine 8 with arginine (H8R) resulted in almost complete loss of infectivity, even though the mutant envelope proteins were stable and efficiently incorporated into virions.”