Poly(ethylene glycol)-conjugation and deoxygenation enable long-term preservation of hemoglobin-vesicles as oxygen carriers in a liquid state

Hiromi Sakai, Ken Ichi Tomiyama, Keitaro Sou, Shinji Takeoka, Eishun Tsuchida

    Research output: Contribution to journalArticle

    100 Citations (Scopus)

    Abstract

    The stability of hemoglobin vesicles (HbV) as an oxygen infusion was tested during the storage for 1 year at 4, 23, and 40 °C. The surface of the HbV was modified with poly(ethylene glycol) (PEG), and the suspension was deoxygenated with nitrogen bubbling. The samples stored at 4 and 23 °C showed a stable dispersion state for 1 year, though the sample stored at 40 °C showed the precipitation and decomposition of vesicular components, a decrease in pH, and 4% leakage of total Hb after 1 year. The PEG chains on the vesicular surface stabilize the dispersion state and prevent the aggregation and fusion due to their steric hindrance. The original metHb content (ca. 3%) before the preservation gradually decreased to less than 1% in all the samples after 1 month due to the presence of homocysteine inside the vesicles which consumed the residual oxygen and gradually reduced the trace amount of metHb. The rate of metHb formation was strongly dependent on the partial pressure of oxygen, and no increase in metHb formation was observed due to the intrinsic stability of the deoxygenated Hb. Preservation at 4 and 23 °C slightly reduced P50 (increased the oxygen affinity) from 38 Torr to 32 and 31 Torr, respectively. These results indicate the possibility that HbV suspension can be stored at room temperature for at least 1 year.

    Original languageEnglish
    Pages (from-to)425-432
    Number of pages8
    JournalBioconjugate Chemistry
    Volume11
    Issue number3
    DOIs
    Publication statusPublished - 2000 May

    Fingerprint

    Ethylene Glycol
    Hemoglobin
    Polyethylene glycols
    Hemoglobins
    Oxygen
    Liquids
    Suspensions
    Partial Pressure
    Homocysteine
    Partial pressure
    Nitrogen
    Fusion reactions
    Agglomeration
    Decomposition
    Temperature

    ASJC Scopus subject areas

    • Chemistry(all)
    • Organic Chemistry
    • Clinical Biochemistry
    • Biochemistry, Genetics and Molecular Biology(all)
    • Biochemistry

    Cite this

    Poly(ethylene glycol)-conjugation and deoxygenation enable long-term preservation of hemoglobin-vesicles as oxygen carriers in a liquid state. / Sakai, Hiromi; Tomiyama, Ken Ichi; Sou, Keitaro; Takeoka, Shinji; Tsuchida, Eishun.

    In: Bioconjugate Chemistry, Vol. 11, No. 3, 05.2000, p. 425-432.

    Research output: Contribution to journalArticle

    @article{8e79f6e2d85a4b70aa68251376a5dc70,
    title = "Poly(ethylene glycol)-conjugation and deoxygenation enable long-term preservation of hemoglobin-vesicles as oxygen carriers in a liquid state",
    abstract = "The stability of hemoglobin vesicles (HbV) as an oxygen infusion was tested during the storage for 1 year at 4, 23, and 40 °C. The surface of the HbV was modified with poly(ethylene glycol) (PEG), and the suspension was deoxygenated with nitrogen bubbling. The samples stored at 4 and 23 °C showed a stable dispersion state for 1 year, though the sample stored at 40 °C showed the precipitation and decomposition of vesicular components, a decrease in pH, and 4{\%} leakage of total Hb after 1 year. The PEG chains on the vesicular surface stabilize the dispersion state and prevent the aggregation and fusion due to their steric hindrance. The original metHb content (ca. 3{\%}) before the preservation gradually decreased to less than 1{\%} in all the samples after 1 month due to the presence of homocysteine inside the vesicles which consumed the residual oxygen and gradually reduced the trace amount of metHb. The rate of metHb formation was strongly dependent on the partial pressure of oxygen, and no increase in metHb formation was observed due to the intrinsic stability of the deoxygenated Hb. Preservation at 4 and 23 °C slightly reduced P50 (increased the oxygen affinity) from 38 Torr to 32 and 31 Torr, respectively. These results indicate the possibility that HbV suspension can be stored at room temperature for at least 1 year.",
    author = "Hiromi Sakai and Tomiyama, {Ken Ichi} and Keitaro Sou and Shinji Takeoka and Eishun Tsuchida",
    year = "2000",
    month = "5",
    doi = "10.1021/bc990173h",
    language = "English",
    volume = "11",
    pages = "425--432",
    journal = "Bioconjugate Chemistry",
    issn = "1043-1802",
    publisher = "American Chemical Society",
    number = "3",

    }

    TY - JOUR

    T1 - Poly(ethylene glycol)-conjugation and deoxygenation enable long-term preservation of hemoglobin-vesicles as oxygen carriers in a liquid state

    AU - Sakai, Hiromi

    AU - Tomiyama, Ken Ichi

    AU - Sou, Keitaro

    AU - Takeoka, Shinji

    AU - Tsuchida, Eishun

    PY - 2000/5

    Y1 - 2000/5

    N2 - The stability of hemoglobin vesicles (HbV) as an oxygen infusion was tested during the storage for 1 year at 4, 23, and 40 °C. The surface of the HbV was modified with poly(ethylene glycol) (PEG), and the suspension was deoxygenated with nitrogen bubbling. The samples stored at 4 and 23 °C showed a stable dispersion state for 1 year, though the sample stored at 40 °C showed the precipitation and decomposition of vesicular components, a decrease in pH, and 4% leakage of total Hb after 1 year. The PEG chains on the vesicular surface stabilize the dispersion state and prevent the aggregation and fusion due to their steric hindrance. The original metHb content (ca. 3%) before the preservation gradually decreased to less than 1% in all the samples after 1 month due to the presence of homocysteine inside the vesicles which consumed the residual oxygen and gradually reduced the trace amount of metHb. The rate of metHb formation was strongly dependent on the partial pressure of oxygen, and no increase in metHb formation was observed due to the intrinsic stability of the deoxygenated Hb. Preservation at 4 and 23 °C slightly reduced P50 (increased the oxygen affinity) from 38 Torr to 32 and 31 Torr, respectively. These results indicate the possibility that HbV suspension can be stored at room temperature for at least 1 year.

    AB - The stability of hemoglobin vesicles (HbV) as an oxygen infusion was tested during the storage for 1 year at 4, 23, and 40 °C. The surface of the HbV was modified with poly(ethylene glycol) (PEG), and the suspension was deoxygenated with nitrogen bubbling. The samples stored at 4 and 23 °C showed a stable dispersion state for 1 year, though the sample stored at 40 °C showed the precipitation and decomposition of vesicular components, a decrease in pH, and 4% leakage of total Hb after 1 year. The PEG chains on the vesicular surface stabilize the dispersion state and prevent the aggregation and fusion due to their steric hindrance. The original metHb content (ca. 3%) before the preservation gradually decreased to less than 1% in all the samples after 1 month due to the presence of homocysteine inside the vesicles which consumed the residual oxygen and gradually reduced the trace amount of metHb. The rate of metHb formation was strongly dependent on the partial pressure of oxygen, and no increase in metHb formation was observed due to the intrinsic stability of the deoxygenated Hb. Preservation at 4 and 23 °C slightly reduced P50 (increased the oxygen affinity) from 38 Torr to 32 and 31 Torr, respectively. These results indicate the possibility that HbV suspension can be stored at room temperature for at least 1 year.

    UR - http://www.scopus.com/inward/record.url?scp=0034090354&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=0034090354&partnerID=8YFLogxK

    U2 - 10.1021/bc990173h

    DO - 10.1021/bc990173h

    M3 - Article

    C2 - 10821660

    AN - SCOPUS:0034090354

    VL - 11

    SP - 425

    EP - 432

    JO - Bioconjugate Chemistry

    JF - Bioconjugate Chemistry

    SN - 1043-1802

    IS - 3

    ER -