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Last Updated: 2 years ago

Possible Interaction: Arginine and Histidine

supplement:

Arginine

supplement:

Histidine

Research Papers that Mention the Interaction

At 1 h post feeding, L-Arg mares had lower (P<0.05) plasma concentrations of histidine , glutamic acid, proline, isoleucine, threonine, phenylalanine, leucine, valine, alanine, and taurine.
Journal of animal science  •  2014  |  View Paper
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).
Nature Structural &Molecular Biology  •  2017  |  View Paper
Moreover, permeability was enhanced as the degrees of substitution of arginine and histidine increased.
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.
Molecular pharmaceutics  •  2014  |  View Paper
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.
The FEBS journal  •  2006  |  View Paper
It is noteworthy that an important role of arginine was identified for regulating agonist-mediated internalization when a histidine (R149H) was present.
Molecular Pharmacology  •  2005  |  View Paper
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.
Biochimica et biophysica acta  •  2000  |  View Paper
Arginine uptake was inhibited strongly by lysine, glutamate, leucine, glutamine, methionine and histidine.
The Biochemical journal  •  2000  |  View Paper
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.
Journal of Virology  •  1999  |  View Paper
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