Die Isolierung von Meerrettichperoxydase.

Paul, K. G.; Studnitz, W. von; Bergson, Göran; Grönvall, A.; Zaar, B.; Diczfalusy, E.

doi:10.3891/acta.chem.scand.12-1312

Cited by 76 publications

(13 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It gave A403/A280 = 4.08 and was homogeneous in polyacryl-I Abbreviations used are: HRP, horseradish peroxidase; Hb, hemoglobin; Mb, myoglobin; ir, infrared; Em7, midpoint potential at pH 7; UCO, wavenumber in cm-l for the CO stretching absorption band; AUCO, the half-bandwidth of this band. (Paul, 1958). At pH 6 the CO complex of this material gave an ir spectrum identical with that of authentic H R P C2.…”

Section: Methodsmentioning

confidence: 59%

Infrared spectroscopic studies of carbonyl horseradish peroxidases

Barlow¹,

Ohlsson²,

Paul³

1976

Biochemistry

View full text Add to dashboard Cite

Infrared difference spectra, FeIIICO vs. FeIII of horseradish peroxidase isoenzymes A2 and C were recorded from 2000 to 1800 cm-1. Under alkaline conditions, pH 9, both isoenzymes exhibit two CO stretching bands, at 1938 and 1925 cm-1 for A2 and at 1933 and 1929 cm-1 for C. As the pH is lowered the low-frequency band for each isoenzyme decreases in intensity with a concommitant appearance and increase in intensity of a band at 1906 and 1905 cm-1 for the A2 and C isoenzymes, respectively. These changes conform to pK values of 6.7 for the A2 and 8.8 for the C isoenzymes of horseradish peroxidase. The interpretation of the infrared results was simplified by the observation that a linear relationship exists between the redox potential, Em7, for the FeIII/FeII system vs. the infrared CO stretching frequency, vCO, for cytochrome a3, hemoglobin, myoglobin, and cytochrome P-450 cam with substrate. This relationship suggests that the primary force altering vCO in these heme proteins is a variation in electron density at the heme iron and not direct protein interactions with the CO ligand. The horseradish peroxidase infrared bands in the 1930-cm-1 region correlate well with this relationship. The large deviation of the 1905-cm-1 band from the linear relationship and its dependence upon hydrogen ion concentration are consistent with horseradish peroxidase having a single CO binding site which can hold in two geometries, one of which contains an amino acid moiety capable of forming a hydrogen bond to the carbonyl oxygen.

show abstract

Section: Methodsmentioning

confidence: 59%

Infrared spectroscopic studies of carbonyl horseradish peroxidases

Barlow¹,

Ohlsson²,

Paul³

1976

Biochemistry

View full text Add to dashboard Cite

show abstract

“…For the protein studies HRP was purchased from Sigma (St. Louis, MO) RZ ϭ 3.0). To purify the basic form (isoenzyme C) of this protein, column chromatography was used (Paul, 1958). The protein was applied to a CM Sepharose (Pharmacia, Piscataway, NJ) in a column equilibrated with 5 mM Tris buffer at pH 7.4 and eluted with 0.01 M NaCl.…”

Section: Sample Preparationsmentioning

confidence: 99%

The Enzyme Horseradish Peroxidase Is Less Compressible at Higher Pressures

Smeller

Fidy

2002

Biophysical Journal

View full text Add to dashboard Cite

Fluorescence line-narrowing (FLN) spectroscopy at 10 K was used to study the effect of high pressure through the prosthetic group in horseradish peroxidase (HRP), which was Mg-mesoporphyrin (MgMP) replacing the heme of the enzyme. The same measurement was performed on MgMP in a solid-state amorphous organic matrix, dimethyl sulfoxide (DMSO). Series of FLN spectra were registered to determine the (0, 0) band shape through the inhomogeneous distribution function (IDF). In the range of 0-2 GPa a red-shift of the IDF was determined, and yielded the isothermal compressibility of MgMP-HRP as 0.066 GPa(-1), which is significantly smaller than that found earlier as 0.106 GPa(-1) by fine-tuning the pressure in the range up to 1.1 MPa. The vibrational frequencies also shifted with pressure increase, as expected. The compressibility in the DMSO matrix was smaller, 0.042 GPa(-1), both when the pressure was applied at room temperature before cooling to 10 K, or at 10 K. At 200 K or above, the bimodal (0, 0) band shape in DMSO showed a population conversion under pressure that was not observed at or below 150 K. A significant atomic rearrangement was estimated from the volume change, 3.3 +/- 0.7 cm(3)/mol upon conversion. The compressibility in proteins and in amorphous solids seems not to significantly depend on the temperature and in the protein it decreases toward higher pressures.

show abstract

“…The rate of reaction with guaiacol ( fig. 1) increases for peroxidase I and decreases for peroxidase III when pH is lowered; at pH 7 the ratio between the k., -values with guaiacol is close to the ratio between the previously reported overall velocities with this substrate [2,4] .…”

Section: Resultsmentioning

confidence: 53%

“…Guaiacol has previously been found to react faster with peroxidase III than with I at pH 7 [2,4]. This observation has now been extended to studies of the reaction rates for some other substrates with the above peroxidases.…”

Section: Introductionmentioning

confidence: 67%