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Journal articles on the topic 'Erythrocruorins'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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1

Musmeci, M. Teresa, and Vincenzo D'Amelio. "Erythrocruorin subunits ofPerinereis cultriferaGrube (Annelida, Polychaeta) compared with other erythrocruorins." Bolletino di zoologia 52, no. 3-4 (1985): 211–17. http://dx.doi.org/10.1080/11250008509440520.

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2

Hendrickson, W. A., and W. E. Royer. "Principles in the assembly of annelid erythrocruorins." Biophysical Journal 49, no. 1 (1986): 177–89. http://dx.doi.org/10.1016/s0006-3495(86)83633-5.

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3

Vinogradov, Serge N. "The structure of invertebrate extracellular hemoglobins (erythrocruorins and chlorocruorins)." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 82, no. 1 (1985): 1–15. http://dx.doi.org/10.1016/0305-0491(85)90120-8.

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4

Zimmerman, Devon, Matthew DiIusto, Jack Dienes, Osheiza Abdulmalik, and Jacob J. Elmer. "Direct comparison of oligochaete erythrocruorins as potential blood substitutes." Bioengineering & Translational Medicine 2, no. 2 (2017): 212–21. http://dx.doi.org/10.1002/btm2.10067.

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5

KLEINSCHMIDT, Traute, Hans-Günther KEYL, and Gerhard BRAUNITZER. "Comparison of Insect Hemoglobins (Erythrocruorins) fromChironomus thummi thummiandChironomus thummi piger (Diptera).The Primary Structure of the Monomeric Hemoglobin CTP III." Biological Chemistry Hoppe-Seyler 370, no. 2 (1989): 839–46. http://dx.doi.org/10.1515/bchm3.1989.370.2.839.

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6

Bridges, C. R., and S. Morris. "Respiratory pigments: interactions between oxygen and carbon dioxide transport." Canadian Journal of Zoology 67, no. 12 (1989): 2971–85. http://dx.doi.org/10.1139/z89-420.

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Oxygen and carbon dioxide are transported in vertebrates and invertebrates by a wide range of respiratory pigments. These respiratory gases are not transported independently of one another, and this review considers the influence of carbon dioxide on oxygen transport and vice versa. A specific effect of carbon dioxide or bicarbonate, decreasing oxygen affinity, is found in many haemoglobins, but the effect is often reduced in the presence of organic phosphates. Clear experimental data are available for mammalian haemoglobins but in birds and lower vertebrates more data are required to verify the presence and magnitude of the CO2 effect. In erythrocruorins and haemocyanins CO2 increases O2 affinity, whereas in haemerythrins, as in haemoglobin, CO2 again decreases oxygen affinity. Much of our knowledge of invertebrate respiratory pigments is based, however, on data from one or two species. A specific effect of CO2 on O2 affinity has also often been found only at high CO2 partial pressures, which may be outside the physiological range for these species. More in vivo experimental data on CO2 values are required for these species, and further studies on other species may help to explain this discrepancy. The interaction of O2 and CO2 transport is mainly through the Haldane effect, i.e., deoxygenated blood having a greater capacity for CO2 than oxygenated blood. This is due directly to the formation of carbamino groups (carbamate) and also to the fact that deoxygenated blood binds relatively more protons than oxygenated blood. This forms the basis for the linkage between the Bohr and Haldane effects. In some species in which the Bohr coefficient is below −1.0, an akalosis in the tissues may be induced. Large Haldane effects may be particularly effective in promoting CO2 unloading when the partial pressure difference of CO2 between arterial and venous blood is small. Carbamate formation may account for 10–20% of the CO2 transported in mammals, but its role in lower vertebrates and invertebrates has only recently been considered. Carbon dioxide transport is modulated by those factors that influence O2 affinity as these in turn influence the Haldane effect.

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7

Darawshe, S., Y. Tsafadyah, and E. Daniel. "Quaternary structure of erythrocruorin from the nematode Ascaris suum. Evidence for unsaturated haem-binding sites." Biochemical Journal 242, no. 3 (1987): 689–94. http://dx.doi.org/10.1042/bj2420689.

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The quaternary structure of erythrocruorin from the nematode Ascaris suum was studied. The native protein had a sedimentation coefficient, at a protein concentration of 1 mg/ml, of 11.6 +/- 0.3 S and an Mr, as determined by sedimentation equilibrium, of 332,000 +/- 17,000. SDS/polyacrylamide-gel electrophoresis gave one band with a mobility corresponding to an Mr of 43,000 +/- 2000. The Mr of the polypeptide chain was determined to be 41,600 +/- 1,500 by sedimentation equilibrium in 6 M-guanidinium chloride and 0.1 M-2-mercaptoethanol. Cross-linking with glutaraldehyde followed by SDS/polyacrylamide-gel electrophoresis yielded a maximal number of eight bands. The haem content of Ascaris erythrocruorin was observed to vary from one preparation to another. This finding was shown to be due to non-realization of the full binding capacity for haem. By titration with haemin, the haem content was found to attain a maximal value of 2.86 +/- 0.14%, corresponding to a minimal Mr per haem group of 21,000 +/- 1,000. Our findings indicate that Ascaris suum erythrocruorin is composed of eight identical polypeptide chains, carrying two haem sites each.

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8

Royer, William E., Wayne A. Hendrickson, and Warner E. Love. "Crystals of Lumbricus erythrocruorin." Journal of Molecular Biology 197, no. 1 (1987): 149–53. http://dx.doi.org/10.1016/0022-2836(87)90618-8.

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9

Royer, W. E., and W. A. Hendrickson. "Molecular symmetry of Lumbricus erythrocruorin." Journal of Biological Chemistry 263, no. 27 (1988): 13762–65. http://dx.doi.org/10.1016/s0021-9258(18)68307-3.

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10

Strand, K., and W. Royer Jr. "Crystallographic investigations of erythrocruorin fromLumbricus terrestris." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (1996): C178. http://dx.doi.org/10.1107/s0108767396092185.

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11

Daniel, Ezra, Ariel Lustig, Melvyn M. David, and Yossi Tsfadia. "On the molecular mass of Lumbricus erythrocruorin." Micron 35, no. 1-2 (2004): 131–32. http://dx.doi.org/10.1016/j.micron.2003.10.042.

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12

Royer, W. E., K. Strand, M. van Heel, and W. A. Hendrickson. "Structural hierarchy in erythrocruorin, the giant respiratory assemblage of annelids." Proceedings of the National Academy of Sciences 97, no. 13 (2000): 7107–11. http://dx.doi.org/10.1073/pnas.97.13.7107.

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13

Timm, Brandon, Osheiza Abdulmalik, Atis Chakrabarti, and Jacob Elmer. "Purification of Lumbricus terrestris erythrocruorin (LtEc) with anion exchange chromatography." Journal of Chromatography B 1150 (August 2020): 122162. http://dx.doi.org/10.1016/j.jchromb.2020.122162.

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14

Vesper, Stephen J., and Mary Jo Vesper. "Stachylysin May Be a Cause of Hemorrhaging in Humans Exposed to Stachybotrys chartarum." Infection and Immunity 70, no. 4 (2002): 2065–69. http://dx.doi.org/10.1128/iai.70.4.2065-2069.2002.

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ABSTRACT Stachybotrys chartarum is a toxigenic fungus that has been associated with human health concerns such as nasal bleeding in adults and pulmonary hemosiderosis (PH) in infants. Seven of eight strains of S. chartarum isolated from homes of infants with PH in Cleveland, Ohio, and the strain from the lung of an infant with PH in Texas produced stachylysin in tryptic soy broth (TSB), whereas only one out of eight strains isolated from control homes produced stachylysin. However, all strains produced stachylysin when grown on TSB with 0.7% sheep's blood. When stachylysin was injected into Lumbricus terrestis, the erythrocruorin hemoglobin (absorbance peaks at 280 and 415 nm) was released, resulting in a lethal effect. These results support the hypothesis that stachylysin may be one agent responsible for hemorrhaging in humans.

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15

Elmer, Jacob, Katie Zorc, Shahid Rameez, Yipin Zhou, Pedro Cabrales, and Andre F. Palmer. "Hypervolemic infusion of Lumbricus terrestris erythrocruorin purified by tangential-flow filtration." Transfusion 52, no. 8 (2012): 1729–40. http://dx.doi.org/10.1111/j.1537-2995.2011.03523.x.

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16

Ilan, Ehud, and Ezra Daniel. "Oxygen binding properties of erythrocruorin from the clam shrimp, Caenestheria inopinata." Comparative Biochemistry and Physiology Part A: Physiology 94, no. 3 (1989): 505–8. http://dx.doi.org/10.1016/0300-9629(89)90129-1.

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17

Barnikol, Wolfgang K. R., Oswald Burkhard, and Harald Pötzchke. "Das Erythrocruorin des Regenwurms (Lumbricus terrestris) als Eichsubstanz in der Gelchromatographie." Journal of Chromatography B: Biomedical Sciences and Applications 497 (January 1989): 231–35. http://dx.doi.org/10.1016/0378-4347(89)80022-2.

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18

schatz, Michael, Joachim Jäger, and Marin van Heel. "Molecular Views of Ice-Embedded Lumbricus Terrestris Erythrocruorin Obtained By Invariant Classification." Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 1 (1990): 450–51. http://dx.doi.org/10.1017/s0424820100181002.

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Lumbricus terrestris erythrocruorin is a giant oxygen-transporting macromolecule in the blood of the common earth worm (worm "hemoglobin"). In our current study, we use specimens (kindly provided by Drs W.E. Royer and W.A. Hendrickson) embedded in vitreous ice (1) to avoid artefacts encountered with the negative stain preparation technigue used in previous studies (2-4).Although the molecular structure is well preserved in vitreous ice, the low contrast and high noise level in the micrographs represent a serious problem in image interpretation. Moreover, the molecules can exhibit many different orientations relative to the object plane of the microscope in this type of preparation. Existing techniques of analysis requiring alignment of the molecular views relative to one or more reference images often thus yield unsatisfactory results.We use a new method in which first rotation-, translation- and mirror invariant functions (5) are derived from the large set of input images, which functions are subsequently classified automatically using multivariate statistical techniques (6). The different molecular views in the data set can therewith be found unbiasedly (5). Within each class, all images are aligned relative to that member of the class which contributes least to the classes′ internal variance (6). This reference image is thus the most typical member of the class. Finally the aligned images from each class are averaged resulting in molecular views with enhanced statistical resolution.

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19

Royer, William E., Hitesh Sharma, Kristen Strand, James E. Knapp, and Balaji Bhyravbhatla. "Lumbricus Erythrocruorin at 3.5 Å Resolution: Architecture of a Megadalton Respiratory Complex." Structure 14, no. 7 (2006): 1167–77. http://dx.doi.org/10.1016/j.str.2006.05.011.

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20

Spivack, Kyle, Matthew Tucker, Devon Zimmerman, et al. "Increasing the stability of Lumbricus terrestris erythrocruorin via poly(acrylic acid) conjugation." Artificial Cells, Nanomedicine, and Biotechnology 46, sup2 (2018): 1137–44. http://dx.doi.org/10.1080/21691401.2018.1480491.

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21

Ellerton, H. David, C. T. Chen, and A. K. Lim. "Subunit structure of the extracellular hemoglobin (erythrocruorin) from the earthworm Lumbricus rubellus." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 87, no. 4 (1987): 1011–16. http://dx.doi.org/10.1016/0305-0491(87)90426-3.

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22

Ilan, Ehud, Ilan Hammel, Melvyn M. David, and Ezra Daniel. "Erythrocruorin from the aquatic snail Helisoma trivolvis. Quaternary structure and arrangement of subunits." Biochemistry 25, no. 21 (1986): 6551–54. http://dx.doi.org/10.1021/bi00369a032.

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23

Cardiilo, F., E. de Paula, G. R. Oliveira, S. Marangoni, B. Oliveira, and N. C. Meirelles. "Erythrocruorin of Glossoscolex paulistus (Oligochaeta, Glossoscolecidae): Modulation of oxygen affinity by specific antibodies." IUBMB Life 41, no. 3 (1997): 497–509. http://dx.doi.org/10.1080/15216549700201521.

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24

Desideri, Alessandro, Emilia Chiancone, and Franca Ascoli. "An EPR Study of NO Bonding to Erythrocruorin from the Earthworm Octolasium Complanatum." Journal of Inorganic Biochemistry 25, no. 3 (1985): 225–28. http://dx.doi.org/10.1016/0162-0134(85)80016-7.

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25

Boekema, Egbert J., and Marin van Heel. "Molecular shape of Lumbricus terrestris erythrocruorin studied by electron microscopy and image analysis." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 957, no. 3 (1988): 370–79. http://dx.doi.org/10.1016/0167-4838(88)90228-2.

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26

Pilz, Ingrid, E. Schwarz, Yossi Tsfadia, and Ezra Daniel. "Small-angle X-ray study on the quaternary structure of erythrocruorin from Helisoma trivolvis." International Journal of Biological Macromolecules 10, no. 6 (1988): 353–55. http://dx.doi.org/10.1016/0141-8130(88)90028-1.

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27

Pilz, Ingrid, Erika Schwarz, Yossi Tsfadia, and Ezra Daniel. "Small-angle X-ray study on the quaternary structure of erythrocruorin from Caenestheria inopinata." International Journal of Biological Macromolecules 13, no. 4 (1991): 222–24. http://dx.doi.org/10.1016/0141-8130(91)90076-7.

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28

Ellerton, H. David, Christine H. Bearman, and Paul C. Loong. "Erythrocruorin from the New Zealand earthworm Maoridrilus montanus: A multi-subunit annelid extracellular hemoglobin." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 87, no. 4 (1987): 1017–23. http://dx.doi.org/10.1016/0305-0491(87)90427-5.

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29

Caracelli, Ignez, Nilce C. Meirelles, Marcel Tabak, Oswaldo Baffa Filho, and Otaciro R. Nascimento. "An ESR study of nitrosyl-Aplysia brasiliana myoglobin and nitrosyl annelidae Glossoscolex paulistus erythrocruorin." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 955, no. 3 (1988): 315–20. http://dx.doi.org/10.1016/0167-4838(88)90210-5.

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30

Roche, Camille J., Abhinav Talwar, Andre F. Palmer, Pedro Cabrales, Gary Gerfen, and Joel M. Friedman. "Evaluating the Capacity to Generate and Preserve Nitric Oxide Bioactivity in Highly Purified Earthworm Erythrocruorin." Journal of Biological Chemistry 290, no. 1 (2014): 99–117. http://dx.doi.org/10.1074/jbc.m114.583260.

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31

Muzzelo, Christine, Christopher Neely, Payal Shah, Osheiza Abdulmalik, and Jacob Elmer. "Prolonging the shelf life of Lumbricus terrestris erythrocruorin for use as a novel blood substitute." Artificial Cells, Nanomedicine, and Biotechnology 46, no. 1 (2017): 39–46. http://dx.doi.org/10.1080/21691401.2017.1290645.

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32

Braunbeck, T., and R. P. Dales. "The Ultrastructure of the Heart-Body and Extravasal Tissue in the Polychaete Annelids Neoamphitrite Figulus and Arenicola Marina." Journal of the Marine Biological Association of the United Kingdom 65, no. 3 (1985): 653–62. http://dx.doi.org/10.1017/s0025315400052498.

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The heart-body in Neoamphitrite figulus (Dalyell) forms a mass of tissue within the supra-oesophageal vessel almost occluding the lumen. The tissue forms a much-infolded cylinder enclosed by a basal lamina consisting of a fibrous reticulum through which the assembled haemoglobin molecules are discharged into the plasma (Dales & Pell, 1970). A function of both the heart-body and the extravasal (‘chloragogen’) tissue in polychaetes without a heart-body was established by biochemical analysis (Kennedy & Dales, 1958; Dales, 1963, 1965) to be the synthesis of plasma haemoglobin (erythrocruorin) or chlorocruorin. This was confirmed by electron microscopy (TEM) by Breton-Gorius (1963) in Arenicola, Potswald (1969) in Spirorbis, Dales & Pell (1970) in Neoamphitrite, Lattice, Myxicola, Megalomma and Sabella, and by Friedmann & Weiss (1980) in Amphitrite. It would appear that the same tissues also sequester phagocytosed materials (Braunbeck & Dales, 1984). Re-examination of this tissue by trans-mission electron microscopy (TEM) has extended our knowledge of the ultra-structure. Here we discuss these results in relation to the function of these tissues in the production of the respiratory pigments found in the plasma. Some heart-bodies of Terebella lapidaria L., Lattice conchilega (Pallas) and Cirriformia tentaculata (Montagu) have also been examined by TEM for comparison with that of Neoamphitrite figulus.

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33

Elmer, Jacob, and Andre F. Palmer. "Biophysical Properties of Lumbricus terrestris Erythrocruorin and Its Potential Use as a Red Blood Cell Substitute." Journal of Functional Biomaterials 3, no. 1 (2012): 49–60. http://dx.doi.org/10.3390/jfb3010049.

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34

Strand, Kristen, James E. Knapp, Balaji Bhyravbhatla, and William E. Royer. "Crystal Structure of the Hemoglobin Dodecamer from Lumbricus Erythrocruorin: Allosteric Core of Giant Annelid Respiratory Complexes." Journal of Molecular Biology 344, no. 1 (2004): 119–34. http://dx.doi.org/10.1016/j.jmb.2004.08.094.

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35

Meirelles, Nilce C., Benedito de Oliveira, Eneida de Paula, Sergio Marangoni, and Maria R. F. Marques. "Erythrocruorin of Glossoscolex paulistus (Oligochaeta, Glossoscolecidade): Presence of disulfide bonds and their relation to ligand properties." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 82, no. 1 (1985): 203–5. http://dx.doi.org/10.1016/0305-0491(85)90153-1.

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36

Abe, Augusto S., and Nilce C. Meirelles. "Oxygen binding properties of erythrocruorin solution and blood PH of the giant earthworm Glossoscolex paulistus (oligochaeta, glossoscolecidae)." Comparative Biochemistry and Physiology Part A: Physiology 80, no. 1 (1985): 53–55. http://dx.doi.org/10.1016/0300-9629(85)90677-2.

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37

Savla, Chintan, and Andre F. Palmer. "Structural Stability and Biophysical Properties of the Mega-Protein Erythrocruorin Are Regulated by Polyethylene Glycol Surface Coverage." Biomacromolecules 22, no. 5 (2021): 2081–93. http://dx.doi.org/10.1021/acs.biomac.1c00196.

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38

Di Iorio, E. E., I. Tavernelli, and W. Yu. "Dynamic properties of monomeric insect erythrocruorin III from Chironomus thummi-thummi: relationships between structural flexibility and functional complexity." Biophysical Journal 73, no. 5 (1997): 2742–51. http://dx.doi.org/10.1016/s0006-3495(97)78303-6.

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39

Marques, M. B., and N. C. Meirelles. "Erythrocruorin of Glossoscolex paulistus (Righi) (Oligochaeta, Glossoscolecidae): effects of divalent ions, acid—Alkaline transition and alkali and urea denaturation." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 111, no. 2 (1995): 311–18. http://dx.doi.org/10.1016/0305-0491(94)00220-o.

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40

Royer, William E., Michael N. Omartian, and James E. Knapp. "Low Resolution Crystal Structure of Arenicola Erythrocruorin: Influence of Coiled Coils on the Architecture of a Megadalton Respiratory Protein." Journal of Molecular Biology 365, no. 1 (2007): 226–36. http://dx.doi.org/10.1016/j.jmb.2006.10.016.

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41

Daniel, Ezra, Ariel Lustig, Melvyn M. David, and Yossi Tsfadia. "Towards a resolution of the long-standing controversy regarding the molecular mass of extracellular erythrocruorin of the earthworm Lumbricus terrestris." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1649, no. 1 (2003): 1–15. http://dx.doi.org/10.1016/s1570-9639(03)00023-2.

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42

Ochiai, Takehiko, and Roy E. Weber. "Effects of Magnesium and Calcium on the Oxygenation Reaction of Erythrocruorin from the Marine Polychaete Arenicola marina and the Terrestrial Oligochaete Lumbricus terrestris." Zoological Science 19, no. 9 (2002): 995–1000. http://dx.doi.org/10.2108/zsj.19.995.

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43

Meirelles, N. C., B. Oliveira, A. R. Oliveira, E. De Paula, S. Marangoni, and G. M. Rennebeck. "Erythrocruorin of Glossoscolex paulistus (oligochaeta, glossoscolecidae): dissociation at alkaline ph and its ligand properties as revealed by chemical, immunochemical and electron microscopy studies." Comparative Biochemistry and Physiology Part A: Physiology 88, no. 2 (1987): 377–79. http://dx.doi.org/10.1016/0300-9629(87)90501-9.

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44

Goodsell, D. S. "Erythrocruorin." RCSB Protein Data Bank, March 1, 2013. http://dx.doi.org/10.2210/rcsb_pdb/mom_2013_3.

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45

García-Flores, Nadia, César Rodríguez-Beas, Ramón Alfonso Iñiguez-Palomares, et al. "Functionalized Liposomes Fabrication and Characterization with Erythrocruorin for a potential application as a Red Blood Cells Substitute." Current Nanoscience 17 (June 20, 2021). http://dx.doi.org/10.2174/1573413717666210620132628.

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Aims: Erythrocruorin for a potential application as a Red Blood Cells Substitute. Background: Nanostructured materials, such as liposomes and polymeric materials have offered new alternatives that allow the design and manufacture of systems as potential substitutes for red blood cells. Objective: Functionalized liposomes Fabrication and Characterization. Methods: The liposomes manufactured with egg yolk lecithin prepared by the extrusion method were functionalized with EfEc and stabilized with polyethylene glycol (PEG) by an absorption method. Results: The nanoplatform has a hydrodynamic diameter of 452.4 ± 24.56 nm; this size provides the ability to avoid problems such as system extravasation, also presents stability (ζ-potential = -30. 06 ± 0.42 mV) and SEM micrographs show a semi-spherical morphology. Also, EfEc showed a peak of fluorescence emission at 449 nm, which allowed us to observe the protein's presence on the surface of the liposomes employing CLSM. Conclusion: In this work, we report the fabrication and characterization of liposomes with EfEc and PEG on their surface. The nanoplatform exhibits physical-chemical characteristics that confer a potential application as a substitute for red blood cells. Other: Microstructural analysis

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