Donald E. Hultquist

Oberlin College, أوبرلين، أوهايو, Ohio, United States

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Publications (48)169.74 Total impact

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    ABSTRACT: Oxidant injury occurs when an organ is severed from its native blood supply and then reperfused and continues during subsequent periods of immune attack. Experiments here test the hypothesis that an antioxidant given only in the peri-reperfusion period protects against not only oxidative but also nitrosative stress, leading to reduced vasculopathy long after cardiac allotransplantation. Experiments were performed using a murine heterotopic cardiac transplantation model. An antioxidant, in the form of intraperitoneal high-dose riboflavin, was given to recipients during the initial 3 days after transplantation. Antioxidant-treated mice showed significantly longer graft survival than control mice. At 4 h after transplantation, antioxidant treatment significantly reduced graft lipid peroxidation and oxidized DNA and preserved antioxidant enzyme activity. At day 6 posttransplantation, the redox-sensitive transcription factor nuclear factor-kappaB and inducible nitric oxide synthase were significantly reduced following antioxidant treatment, with concomitant reduction of nitrotyrosine. Despite the limited duration of antioxidant treatment, both acute and chronic rejection were significantly suppressed. In vitro experiments confirmed suppression of nitrosative and oxidative stress and cardiomyocyte damage in antioxidant-treated cardiac allografts. Collectively, antioxidant administration during the initial 3 days after transplantation significantly reduces nitrosative and oxidative stress in cardiac allografts, modulates immune responses, and protects against vasculopathy.
    AJP Heart and Circulatory Physiology 02/2009; 296(4):H1007-16. DOI:10.1152/ajpheart.00498.2008 · 3.84 Impact Factor
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    ABSTRACT: Riboflavin is a well-known nutritional supplement that has been shown to exhibit antioxidant properties and protect tissue from oxidative damage. We hypothesized that riboflavin given during cardiac ischemia-reperfusion (I/R) might reduce subsequent acute rejection, after allotransplantation, and coronary allograft vasculopathy (CAV). A murine heterotopic cardiac transplantation model was used to test whether riboflavin improves I/R injury and acute/chronic rejection. Riboflavin significantly reduced oxidant production and inflammatory mediator production induced by I/R injury, as evidenced by decreased levels of malondialdehyde, myeloperoxidase activity, and tumor necrosis factor alpha. Administration of riboflavin also improved graft survival and suppressed T-cell infiltration and donor-reactive alloantibody formation during the early period after allotransplantation. A murine long-term cardiac allograft model using immunosuppression (preoperative anti-murine CD4 and anti-CD8) was employed to investigate the effect of riboflavin against CAV at 60 days. Riboflavin-treated grafts exhibited a significant decrease in the severity of coronary artery luminal occlusion as compared with saline-treated grafts (17.4+/-1.8% vs. 43.5+/-5.6%, P=0.0012). However, there was no significant effect of riboflavin to reduce donor-reactive alloantibodies in this chronic model. These data indicate that riboflavin improves early I/R injury and reduces the development of CAV, most likely due to alloantigen-independent effects such as reduced early graft oxidant stress. Riboflavin administered in the setting of cardiac allograft transplantation appears to be a powerful means to reduce early graft lipid peroxidation, leukocytic infiltration, and cytokine production as well as to suppress the late development of cardiac allograft vasculopathy.
    Transplantation 04/2007; 83(6):747-53. DOI:10.1097/ · 3.83 Impact Factor
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    Andreas Seekamp · Donald E. Hultquist · Gerd O. Till ·
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    ABSTRACT: The effect of vitamin B2 (riboflavin) on oxidant-mediated acute lung injury has been examined in three different rat models. Pulmonary injury was induced by intravenous injection of cobra venom factor (CVF), by the intrapulmonary deposition of IgG immune complexes, or by hind limb ischemia-reperfusion. In each of the three models, injury was characterized by increases in vascular permeability (leakage of 125I-labeled bovine serum albumin), alveolar hemorrhage (extravasation of 51Cr-labeled rat erythrocytes), and neutrophil accumulation (myeloperoxidase activity). Intraperitoneal administration of riboflavin at a dose of 6 micromoles/kg body weight reduced vascular leakage by 56% in the CVF model, by 31% in the immune complex model, and by 53% in the lung injury model following ischemia-reperfusion of the hind limbs. Similar treatment reduced hemorrhage by 76%, 51%, and 70% in the three models of lung injury. In the CVF model, riboflavin was also shown to decrease products of lipid peroxidation (conjugated dienes) in lungs (by 45%) and in plasma (by 74%). Neutrophil accumulation in the lungs was not influenced by riboflavin administration in any of the three models. The studies demonstrate that riboflavin can mount a significant protection against oxidant-mediated inflammatory organ injury.
    Inflammation 11/1999; 23(5):449-60. DOI:10.1023/A:1021965026580 · 2.21 Impact Factor
  • C P Mack · D E Hultquist · M Shlafer ·
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    ABSTRACT: Ferrylmyoglobin has been implicated in cardiac reoxygenation damage. Flavin reductase, an enzyme previously isolated from erythrocytes, can reduce ferrylmyoglobin in the presence of sufficient flavin concentrations. Flavin reductase mRNA signals were detected in rabbit heart, lung, liver, kidney, and isolated cardiomyocytes. It was hypothesized that increasing flavin reductase catalysis by administering flavins exogenously could decrease cardiac reoxygenation damage in isolated rabbit hearts. Riboflavin (150 microM) inhibited reoxygenation-induced lactate dehydrogenase release by 57%, an effect prevented by hematoporphyrin, a flavin reductase inhibitor. The results suggest that riboflavin supplementation has cardioprotective effects during reoxygenation and that these effects are mediated by flavin reductase.
    Biochemical and Biophysical Research Communications 08/1995; 212(1):35-40. DOI:10.1006/bbrc.1995.1932 · 2.30 Impact Factor
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    K S Quandt · D E Hultquist ·
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    ABSTRACT: Flavin reductase catalyzes electron transfer from reduced pyridine nucleotides to methylene blue or riboflavin, and this catalysis is the basis of the therapeutic use of methylene blue or riboflavin in the treatment of methemoglobinemia. A cDNA for a mammalian flavin reductase has been isolated and sequenced. Degenerate oligonucleotides, with sequences based on amino acid sequences of peptides derived from bovine erythrocyte flavin reductase, were used as primers in PCR to selectively amplify a partial cDNA that encodes the bovine reductase. The template used in the PCR was first strand cDNA synthesized from bovine liver total RNA using oligo(dT) primers. A PCR product was used as a specific probe to screen a bovine liver cDNA library. The sequence determined from two overlapping clones contains an open reading frame of 621 nucleotides and encodes 206 amino acids. The amino acid sequence deduced from the bovine liver flavin reductase cDNA matches the amino acid sequences determined for erythrocyte reductase-derived peptides, and the predicted molecular mass of 22,001 Da for the liver reductase agrees well with the molecular mass of 21,994 Da determined for the erythrocyte reductase by electrospray mass spectrometry. The amino acid sequence at the N terminus of the reductase has homology to sequences of pyridine nucleotide-dependent enzymes, and the predicted secondary structure, beta alpha beta, resembles the common nucleotide-binding structural motif. RNA blot analysis indicates a single 1-kilobase reductase transcript in human heart, kidney, liver, lung, pancreas, placenta, and skeletal muscle.
    Proceedings of the National Academy of Sciences 10/1994; 91(20):9322-6. DOI:10.1073/pnas.91.20.9322 · 9.67 Impact Factor
  • A. Lorris Betz · X D Ren · S R Ennis · D E Hultquist ·
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    ABSTRACT: Oxidized irwN has been proposed as a mediator of the free radical-induced damage that occurs during cerebral ischemia. Dihydroriboflavin, a compound produced from riboflavin (B2) by NADPH-dependent flavin reductase, rapidly reduces oxidized iron. Since treatment with riboflavin offers protection from ischemic injury in other tissues, we tested the effect of pretreatment with B2 on brain edema formation during focal ischemia. Two different models of middle cerebral artery occlusion (MCAO) in rats were tested: transcranial electrocautery and intracarotid occlusion with a nylon thread. Groups of 6-8 animals were treated with 7.5 mg of B2/kg or saline vehicle 1 h before MCAO and brain water content was determined after 4 h of ischemia. Pretreatment with B2 reduced total hemisphere edema formation from 0.37 +/- 0.05 to 0.19 +/- 0.05 mg/g dry wt. (48% protection, p < 0.01) following transcranial MCAO. Edema was greater following MCAO with the intra-carotid thread (0.54 +/- 0.05 ml/g) but protection by B2 was less (21%). We conclude that pretreatment with B2 reduces ischemic brain injury, perhaps by reacting with oxidized iron. However, the larger stroke produced by the thread MCAO method makes it more difficult to observe protection following brief ischemia in this model.
    Acta neurochirurgica. Supplement 01/1994; 60:314-7. DOI:10.1007/978-3-7091-9334-1_84
  • Donald E. Hultquist · Christopher P. Mack · Kim S. Quandt · Marshal Shlafer · Feng Xu ·

    Free Radical Biology and Medicine 11/1993; 15(5):489. DOI:10.1016/0891-5849(93)90254-R · 5.74 Impact Factor
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    F Xu · C.P. Mack · K.S. Quandt · M Shlafer · V Massey · D.E. Hultquist ·
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    ABSTRACT: Pyrroloquinoline quinone has been isolated from bacteria and recently has been detected in mammalian tissues and fluids. We report in vitro studies which show that pyrroloquinoline quinone serves as a high-affinity substrate for an erythrocyte "flavin reductase" and that the pyrroloquinoline quinol generated by this catalysis reacts rapidly with ferryl myoglobin radical. Western blot analysis of rat and rabbit heart homogenates detects a cross-reactive protein which has a molecular weight identical to the erythrocyte reductase from the same species. Low concentrations of pyrroloquinoline quinone protect isolated rabbit heart from re-oxygenation injury, serving as an effective tissue-protective agent in this model for cellular oxidative damage. We propose that this tissue protection is due to a pyrroloquinoline quinol-mediated reduction of reactive oxygen species.
    Biochemical and Biophysical Research Communications 06/1993; 193(1):434-9. DOI:10.1006/bbrc.1993.1642 · 2.30 Impact Factor
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    F Xu · Louis J. DeFilippi · D.P. Ballou · D.E. Hultquist ·
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    ABSTRACT: The ferric and ferrous forms of bovine erythrocyte green hemeprotein react with hydroperoxides to form higher oxidation state intermediates with absorbance maxima in the Soret region at 426 and 422 nm, respectively. In the absence of an appropriate reductant, these intermediates undergo rapid bleaching reactions. 2,2'-Azinobis(3-ethylbenzthiazoline-6-sulfonic acid) rapidly reduces the intermediate formed by reaction of ferric green hemeprotein with hydrogen peroxide, thereby preventing bleaching and allowing the rate of the intermediate formation to be calculated from the coupled dye oxidation. This rate constant of 70 M-1 s-1 at 23 degrees C is similar to those determined by bleaching and by direct photometric detection of the intermediate. Dihydroriboflavin rapidly reduces the intermediate formed by reaction of ferrous green hemeprotein with hydrogen peroxide, thereby preventing bleaching and allowing the rate of the intermediate formation to be calculated from the coupled dihydroriboflavin oxidation; the rate constant of 2 x 10(4) M-1 s-1 at 23 degrees C is similar to the value calculated by direct detection of the intermediate. The results demonstrate that, in contrast to the reductase activity of its heme-free form, the green heme form of the protein reacts with hydroperoxides to generate highly unstable peroxide complexes.
    Archives of Biochemistry and Biophysics 03/1993; 301(1):184-9. DOI:10.1006/abbi.1993.1131 · 3.02 Impact Factor
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    ABSTRACT: NADPH-dependent methemoglobin reductase, first detected in erythrocytes sixty years ago, has subsequently been purified and characterized as a methylene blue reductase and a flavin reductase. The reductase plays no role in methemoglobin reduction under normal conditions, but its activity serves as the basis for the treatment of methemoglobinemia with methylene blue or flavin. On-going studies demonstrate that this cytosolic protein is also present in liver and that its primary structure distinguishes it from other known proteins. The bovine erythrocyte reductase tightly binds hemes, porphyrins, and fatty acids with resulting loss of activity. Pyrroloquinoline quinone serves as a high-affinity substrate of the reductase, suggesting that this naturally-occurring compound may be a physiological substrate. The ability of the reductase to catalyze the intracellular reduction of administered riboflavin to dihydroriboflavin suggested that this system might be exploited to protect tissues from oxidative damage. This hypothesis was supported by our finding that dihydroriboflavin reacts rapidly with Fe(IV)O and Fe(V)O oxidation states of hemeproteins, states that have been implicated in tissue damage associated with ischemia and reperfusion. Preliminary studies demonstrate that, as predicted, administration of low concentrations of riboflavin protects isolated rabbit heart from reoxygenation injury, rat lung from injury resulting from systemic activation of complement, and rat brain from damage caused by four hours of ischemia. Data from these animal studies suggest that flavin therapy holds promise in protecting tissue from the oxidative injuries of myocardial infarction, acute lung injury, stroke, and a number of other clinical conditions.
    American Journal of Hematology 01/1993; 42(1):13-8. DOI:10.1002/ajh.2830420105 · 3.80 Impact Factor
  • F Xu · D E Hultquist ·
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    ABSTRACT: Glutathione S-transferase has been purified from bovine erythrocytes by affinity chromatography. The enzyme has an isoelectric point of 7.2, behaves as a 48-kDa protein composed of two identical subunits, and has an N-terminal sequence of PPYTIVYFPVQGR?EAMRMLL. This sequence, the amino acid composition, and the kinetic parameters suggest that the enzyme belongs to the pi-class of transferases. Hemins, porphyrins, and fatty acids form complexes with the enzyme and serve as effective inhibitors. Treatment of the transferase with N-ethylmaleimide, 3-amino-1,2,4-triazole, diethyl pyrocarbonate, or 2,3-butanedione inhibits transferase activity without altering tetrapyrrole binding. The role of the complexation and inhibition of glutathione S-transferase in erythroid metabolism has yet to be elucidated.
    Biochemistry international 08/1992; 27(2):265-74.
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    F Xu · K S Quandt · D E Hultquist ·
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    ABSTRACT: An NADPH-dependent reductase, first shown in the 1930s to catalyze the methylene blue-dependent reduction of methemoglobin in erythrocytes, has now been characterized as a high-affinity heme-binding protein and has been detected in liver. Highly purified bovine erythrocyte reductase binds protohemin to form a 1:1 complex with a Kd of 7 nM. Binding of protohemin completely inhibits reductase activity. Other tetrapyrroles and fatty acids also bind to the reductase and inhibit its activity. Protoporphyrin, hematoporphyrin, and coproporphyrin form 1:1 complexes with Kd values ranging from 1 to 5 microM. The inhibition constants for a number of saturated and unsaturated fatty acids range from 6 to 52 microM. A protein that is immunologically cross-reactive to the reductase has been detected in the cytosolic fractions of bovine and rat liver and of bovine, rat, rabbit, and human erythrocytes. By immunoblot analysis, the bovine liver and erythrocyte proteins appear identical in size, as do the rat liver and erythrocyte proteins. The concentration of the protein in bovine erythrocytes has been estimated by quantitative immunoblotting to be 10 microM. The detection of this protein in liver cells, the demonstration of its binding properties, and its weak reductase activity bring into question the long-held belief that this is uniquely an erythrocyte protein and that it functions as a reductase.
    Proceedings of the National Academy of Sciences 04/1992; 89(6):2130-4. DOI:10.1073/pnas.89.6.2130 · 9.67 Impact Factor
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    Xu Feng · Donald E. Hultquist ·
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    ABSTRACT: The reactions between hydrogen peroxide and hemeproteins have been coupled to the oxidation of dihydroriboflavin so as to provide a simple method for measuring the rate constant of hemeprotein peroxidation. Dihydroriboflavin rapidly reduces the higher oxidation states of iron and the hydroxy radicals which are the products of the hemeprotein / hydrogen peroxide reaction. The rapid reduction of these highly reactive compounds prevents the hemeproteins from undergoing irreversible chemical modifications and thus allows the kinetics of peroxidation to be studied. The rate constants at pH 7.2 and 23°C for the peroxidation of horseradish peroxidase, myoglobin, and ferrocytochrome c are found to be 6.2 × 106, 7.5 × 104, and 8 × 103M−1s−1, respectively. These studies suggest that reduced riboflavin might efficiently protect cells from oxidative damage such as that occurring in inflammation and reperfusion injury.
    Biochemical and Biophysical Research Communications 12/1991; 181(1-181):197-203. DOI:10.1016/S0006-291X(05)81401-9 · 2.30 Impact Factor
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    Kim S. Quandt · Feng Xu · Ping Chen · Donald E. Hultquist ·
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    ABSTRACT: Bovine erythrocyte green heme binding protein and bovine erythrocyte flavin reductase have been isolated in highly purified forms and subjected to amino acid analysis and N-terminal amino acid sequence analysis. The two proteins possess similar amino acid compositions and identical N-terminal amino acid sequences. Moreover, the two proteins are immunochemically cross-reactive and are indistinguishable when compared by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by double diffusion technique. This study provides evidence that the protein components of bovine erythrocyte green heme binding protein and flavin reductase are identical.
    Biochemical and Biophysical Research Communications 08/1991; 178(1):315-21. DOI:10.1016/0006-291X(91)91816-U · 2.30 Impact Factor
  • Toshitsugu Yubisui · Masazumi Takeshita · Donald E. Hultquist ·
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    ABSTRACT: Methemoglobin reduction was shown to proceed much more rapidly in erythroid cells from rat bone marrow than in rat erythrocytes. Methemoglobin reduction in suspensions of intact, nitrite-treated bone marrow cells does not depend on the presence of glucose in the incubation mixture, even after the cells have been stored in substrate-free medium. 2-Deoxyglucose and iodoacetate prevent the reduction from proceeding to completion. The results suggest that, relative to erythrocytes, immature erythroid cells more efficiently catalyze methemoglobin reduction and more effectively store metabolites which provide electrons for this reaction.
    American Journal of Hematology 05/1990; 34(1):5-7. DOI:10.1002/ajh.2830340103 · 3.80 Impact Factor
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    David A. Juckett · Donald E. Hultquist ·
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    ABSTRACT: The final step in the erythrocyte methemoglobin reduction pathway, the transfer of an electron from cytochrome b5 to methemoglobin, has been studied using magnetic circular dichroism spectroscopy. Spectral analysis allowed us to determine accurately the concentration of each redox species in mixtures of the two heme-proteins and to follow simultaneously the kinetics of the appearance or disappearance of each of these species during reduction reactions. Our analysis detected a substantial increase in the high-spin hydroxymethemoglobin species in the partially reduced bovine hemoglobin tetramer. This species was sensitive to the degree of reduction and pH, and was spectrally similar to fluoride methemoglobin. At pH 7.8, 100% of the hydroxide component of methemoglobin was in the high-spin form when two or more subunits were in the ferrous form. Kinetic analysis of bovine methemoglobin reduction yielded values for the apparent first-order rates for the tetrameric species possessing four, three, two, and one ferric subunit. Further analysis showed that the reduction kinetics can also be described by an equilibrium state, pure competitive inhibition model for enzyme catalysis in which ferrous and ferric subunits of hemoglobin compete for cytochrome b5. This analysis generated a KD that depends on ionic strength and hemoglobin tetramer conformation, a Vmax that was independent of these factors, and an inhibition constant that was equal to KD. This model is consistent with the hypothesis that the reduction of methemoglobin can be separated into two steps, the ionic interaction between cytochrome b5 and hemoglobin and the electron transfer.
    Biophysical Chemistry 07/1984; 19(4):321-35. DOI:10.1016/0301-4622(84)87015-5 · 1.99 Impact Factor
  • D E Hultquist · L J Sannes · D A Juckett ·

    Current topics in cellular regulation 02/1984; 24:287-300.
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    Dorothy A. Schafer · Donald E. Hultquist ·
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    ABSTRACT: A single form of cytochrome b5 has been isolated in highly purified form from the cytosolic fraction of rabbit erythrocytes by sequential chromatography on DE-52 cellulose, Sephadex G-75, and DEAE-Sephadex A50. The cytochrome is structurally similar to the N-terminal, heme-binding domain of rabbit liver microsomal cytochrome b5. Like the liver protein, it is blocked at the amino terminus. Its amino acid composition is similar to that of residues 1-97 of the microsomal protein. With one exception, tryptic peptides derived from apo-cytochrome b5 of rabbit erythrocytes co-elute with the tryptic peptides obtained from a soluble hemepeptide fragment of microsomal cytochrome b5. These findings, together with amino acid sequence analysis of the carboxyl terminal tryptic peptides, identify the erythrocyte cytochrome b5 as a 97-residue peptide.
    Biochemical and Biophysical Research Communications 10/1983; 115(3):807-13. DOI:10.1016/S0006-291X(83)80006-0 · 2.30 Impact Factor
  • D A Juckett · D E Hultquist ·
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    ABSTRACT: Affinity chromatography with immobilized transferrin has been used to effect a partial purification of erythroblasts and reticulocytes from bone marrow. Human transferrin was covalently attached to Sepharose CL-2B, Bio-Gel A-1.5, A-0.5, P-20, P-6, P-4, and P-2, and Sephadex G-75. Nucleated erythroid cells bound to the greatest degree to the polyacrylamide P-6 bead, whereas reticulocytes had the greatest affinity for the Sepharose CL-2B bead. The polyacrylamide P-6 bead has a greater density of surface groups than the Sepharose bead, and this correlates to the greater density of transferrin receptors on erythroblasts. The beads were used in a column which contained a central stirring bar with multiple crosspieces. The stirrer provided a method to uniformly agitate the beads to facilitate elution of the cells bound to the matrix. Approximately 1-2 x 10(8) bone marrow cells could be applied to a 25-ml matrix bed. This procedure resulted in a considerable resolution of cell types and gave a high yield of reticulocytes and erythroblasts from rat and rabbit bone marrow.
    Proceedings of The Society for Experimental Biology and Medicine 02/1983; 172(1):79-83. DOI:10.3181/00379727-172-41530
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    Shelley R. Slaughter · Charles H. Williams · Donald E. Hultquist ·
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    ABSTRACT: A structural comparison has been made between bovine erythrocyte cytochrome b5 and solubilized forms of bovine hepatic microsomal cytochrome b5. Two soluble forms of microsomal cytochrome b5 (designated Forms A and B) were generated by digestion of microsomes with a crude hepatic lysosomal cathepsin preparation and purified by successive chromatography on DEAE-cellulose,Bio-Gel P-60 and DEAE-Sephadex A-50.Amino acid analyses and terminal residue analyses identified Form A as the segment corresponding to residues 1∗95 of the native microsomal protein and Form B as the segment corresponding to residues 1∗107. Erythrocyte cytochrome b5 I was shown to be a protein which corresponds to a segment of the hepatic microsomal molecule containing residues 1∗97, whereas erythrocyte cytochrome b5 II is a protein corresponding to residues 1∗95. Like the native microsomal cytochrome and the cathepsin-solubilized forms of the cytochrome, no amino terminal residue could be detected in the erythrocyte cytochrome.Carboxypeptidases A and B released from erythrocyte Form I a residue eluting at the position of serine, but released no residue from Form II. The results are consistent with serine being the residue at position 97 of the native microsomal protein, and proline and serine being the residues in positions 94 and 95, respectively. The maps of the tryptic peptides derived from the apoprotein forms of erythrocyte cytochrome b5 I and II and cathepsin-solubilized microsomal Forms A and B were very similar, with eight of the expected twelve peptides displaying the same mobility on every map. Amino acid analyses of the isolated tryptic peptides from erythrocyte Form I and hepatic Form B confirmed the structural assignments of these proteins. These data demonstrate that the soluble forms of erythrocyte cytochrome b5 correspond to hydrophilic segments of the native membrane-bound microsomal cytochrome b5 and suggest that the hepatic lysosomal proteases serve as a good model for the putative erythroid proteases which solubilize microsomal cytochrome b5 during erythroid maturation.
    Biochimica et Biophysica Acta 08/1982; 705(2):228-37. DOI:10.1016/0167-4838(82)90182-0 · 4.66 Impact Factor

Publication Stats

954 Citations
169.74 Total Impact Points


  • 2009
    • Oberlin College
      • Department of Chemistry / Biochemistry
      أوبرلين، أوهايو, Ohio, United States
  • 1979-1999
    • Concordia University–Ann Arbor
      Ann Arbor, Michigan, United States
  • 1971-1995
    • University of Michigan
      • • Department of Biological Chemistry
      • • Department of Neurology
      Ann Arbor, Michigan, United States
  • 1980
    • The University of Chicago Medical Center
      Chicago, Illinois, United States
  • 1970
    • City of Hope National Medical Center
      Duarte, California, United States