Subunit interactions of Glycera dibranchiata hemoglobin.

Harrington, John P.; Suárez, Gustavo; Borgese, Thomas A.; Nagel, Ronald L.

doi:10.1016/s0021-9258(17)37993-0

Cited by 24 publications

(3 citation statements)

References 30 publications

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“…This behavior is also exhibited by myoglobin (vide infra). Although this multiple line behavior was indicated in the only IEF gel figure yet published (Kandler & Satterlee, 1983), the actual complexity is belied by tabulated or descriptive reports of IEF experiments (Cooke & Wright, 1985a;Parkhurst et al, 1980;Weber et al, 1977;Harrington et al, 1978). Clearly, development of a purity criterion is essential to further work with these proteins and, as will become obvious later, to understanding the NMR-detected heterogeneity, which is shown to be a phenomenon not related to the globin homogeneity of the Glycera monomer hemoglobin preparations.…”

Section: Resultsmentioning

confidence: 97%

“…Padlan & Love, 1974;Seamonds et al, 1971aSeamonds et al, ,b, 1976;Weber et al, 1977;Harrington et al, 1978;Hoffman & Mangum, 1970;Seamonds & Forster, 1972;Seamonds, 1971;Satterlee, 1983) little high-resolution purification was carried out until recently(Kandler & Satterlee, 1983; Kandler et al, 1984; Cooke & Wright, 1985; Parkhurst et al, 1980). Still, however, we have remained the only group to have published high-©…”

mentioning

confidence: 99%

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Isoelectric focusing purity criteria and proton NMR detectable spectroscopic heterogeneity in the major isolated monomer hemoglobins from Glycera dibranchiata

Constantinidis¹,

Satterlee²

1987

Biochemistry

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Section: Resultsmentioning

confidence: 97%

mentioning

confidence: 99%

Isoelectric focusing purity criteria and proton NMR detectable spectroscopic heterogeneity in the major isolated monomer hemoglobins from Glycera dibranchiata

Constantinidis¹,

Satterlee²

1987

Biochemistry

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“…Several other investigators (Bailey et al, 1979;Glanville et al, 1979;Kresina & Miller, 1979;Sage et al, 1979) reported on the presence of at least two types of genetically distinct chains, designated C and D chains,1 in placenta, a tissue rich in basement membrane. Our laboratory also described isolation of the C and D chains from anterior lens capsule and glomerular basement membrane (Dixit, 1978, 1979Dixit & Kang, 1979). The results of biosynthetic investigations on the basement membrane of murine tumor (Timpl et al, 1978)…”

Section: Resultsmentioning

confidence: 99%

Kinetics of oxygen and carbon monoxide binding to the hemoglobins of Glycera dibranchiata

Parkhurst¹,

Sima

Goss

1980

Biochemistry

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Direct comparison of oligochaete erythrocruorins as potential blood substitutes

Zimmerman

DiIusto

Dienes

et al. 2017

Bioengineering & Transla Med

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While many blood substitutes are based on mammalian hemoglobins (e.g., human hemoglobin, HbA), the naturally extracellular hemoglobins of invertebrates (a.k.a. erythrocruorins, Ecs) are intriguing alternative oxygen carriers. Specifically, the erythrocruorin of Lumbricus terrestris has been shown to effectively deliver oxygen in mice and rats without the negative side effects observed with HbA. In this study, the properties of six oligochaete Ecs (Lumbricus terrestris, Eisenia hortensis, Eisenia fetida, Eisenia veneta, Eudrilus eugeniae, and Amynthas gracilis) were compared in vitro to identify the most promising blood substitute candidate(s). Several metrics were used to compare the Ecs, including their oxidation rates, dissociation at physiological pH, thermal stability, and oxygen transport characteristics. Overall, the Ecs of Lumbricus terrestris (LtEc) and Eisenia fetida (EfEc) were identified as promising candidates, since they demonstrated high thermal and oligomeric stability, while also exhibiting relatively low oxidation rates. Interestingly, the O2 affinity of LtEc (P 50 = 26.25 mmHg at 37 °C) was also observed to be uniquely lower than EfEc and all of the other Ecs (P 50 = 9.29–13.62 mmHg). Subsequent alignment of the primary sequences of LtEc and EfEc revealed several significant amino acid substitutions within the D subunit interfaces that may be responsible for this significant change in O2 affinity. Nonetheless, these results show that LtEc and EfEc are promising potential blood substitutes that are resistant to oxidation and denaturation, but additional experiments will need to be conducted to determine their safety, efficacy, and the effects of their disparate oxygen affinities in vivo.

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Subunit interactions of Glycera dibranchiata hemoglobin.

Cited by 24 publications

References 30 publications

Isoelectric focusing purity criteria and proton NMR detectable spectroscopic heterogeneity in the major isolated monomer hemoglobins from Glycera dibranchiata

Isoelectric focusing purity criteria and proton NMR detectable spectroscopic heterogeneity in the major isolated monomer hemoglobins from Glycera dibranchiata

Kinetics of oxygen and carbon monoxide binding to the hemoglobins of Glycera dibranchiata

Direct comparison of oligochaete erythrocruorins as potential blood substitutes

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