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Hovorka, Susan W.; Biesiada, Homigol; Williams, Todd D.; Hühmer, Andreas; Schöneich, Christian

doi:10.1023/a:1015164200431

Cited by 19 publications

(13 citation statements)

References 15 publications

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“…6,8 There are some reports on the binding properties and structural changes of hGH due to its interaction with metal ions. [9][10][11][12] The metal-binding site in hGH is located in the hydrophobic core. A well-resolved crystal structure of hGH has been obtained, showing that the metal-binding site is likely composed of 18 His and 21 His on helix I and 174 Glu on helix IV.…”

Section: Introductionmentioning

confidence: 99%

A thermodynamic study on the interaction between magnesium ion and human growth hormone

et al. 2005

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A thermodynamic study on the interaction between magnesium ion and human growth hormone (hGH) was studied at 27 degrees C in NaCl solution (50 mM) using different techniques. Two techniques of ionmetry using a Mg2+selective membrane electrode and isothermal titration calorimetry were applied to obtain the binding isotherm for hGHMg2+; results obtained by both techniques were found to be in good agreement. There is a set of three identical and noninteracting binding sites for magnesium ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 46 microM and -17.7 kJ/mol, respectively. Temperature scanning UV-visible spectroscopy was applied to elucidate the effect of Mg2+ binding on the protein stability, and circular dichroism (CD) spectroscopy was used to show the structural change of hGH due to the metal ion interaction. Magnesium ion binding increased the protein thermal stability by increasing the alpha-helix content as well as decreasing both beta and random coil structures. However, the secondary structural change of the protein returns to its native form, including a small change in the tertiary structure, in high concentrations of magnesium ion.

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Section: Introductionmentioning

confidence: 99%

A thermodynamic study on the interaction between magnesium ion and human growth hormone

et al. 2005

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“…According to Hovorka et al, 21 the B chain of the insulin monomer contains two histidine (His) residues, 5 HisB and 10 HisB. Three insulin dimers aggregate in the presence of zinc ions into a torus-shaped hexamer with two zinc-binding sites.…”

Section: Determination Of Zinc In Izs Injection Using Alkaline Phosphmentioning

confidence: 99%

“…21 injection was studied. It was found necessary to keep the concentration of hydrochloric acid (introduced with the insulin sample) as low as possible in order to avoid a shift of the pH optimum value and considerable inhibition (I > 25%) of the catalytic activity of ALPIII by chloride ions.…”

Section: Determination Of Zinc In Izs Injection Using Alkaline Phosphmentioning

confidence: 99%

“…Thus, it is necessary to control the zinc content in IZS to guarantee their high quality and therapeutic usefulness. 20,21 Recently estimating Mg-deficiency has become of considerable interest. This disease may be caused by different reasons (imbalanced diet, stress, physical efforts or hypodinamiya, alcoholism, hormonal contraception, reception of diuretics, etc.…”

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confidence: 99%

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Application of Alkaline Phosphatases from Different Sources in Pharmaceutical and Clinical Analysis for the Determination of Their Cofactors; Zinc and Magnesium Ions

et al. 2007

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“…There are some reports on the binding properties and structural changes of hGH due to its interaction with metal ions [9][10][11][12]. Metal-binding site in hGH is located in the hydrophobic core.…”

Section: Introductionmentioning

confidence: 99%

Effects of calcium binding on the structure and stability of human growth hormone

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Atri

Sanati

et al. 2005

International Journal of Biological Macromolecules

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Abstract: At a Zn2+/INS molar ratio comparable to that in regular INS preparations, Zn2+-INS was susceptible to MCO. Both His residues of INS were converted partially to 2-oxo-His, with 10His(B) possessing ca. three times greater susceptibility to MCO than 5His(B).

Cited by 19 publications

References 15 publications

A thermodynamic study on the interaction between magnesium ion and human growth hormone

A thermodynamic study on the interaction between magnesium ion and human growth hormone

Application of Alkaline Phosphatases from Different Sources in Pharmaceutical and Clinical Analysis for the Determination of Their Cofactors; Zinc and Magnesium Ions

Effects of calcium binding on the structure and stability of human growth hormone

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