The Molecular Weight of Erythrocruorin

Svedberg, The; Eriksson, Inga-Britta

doi:10.1021/ja01334a033

Cited by 98 publications

(23 citation statements)

References 2 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Despite the fact that HbLt has been extensively studied over the past 20 years, the issue of its true MM is still not fully understood. HbLt was one of the proteins studied by Theodore Svedberg and collaborators in 1933 [16], and later work by Daniel et al has argued that the MM of HbLt could vary between 3.6 and 4.4 MDa [17]. They propose a model for the whole protein, consisting of twelve equal structures involving a dodecamer, (abcd) 3 , and three linkers L 3 , together with twelve tetramers (abcd), in such a way that the protomer corresponding to the 1/12 of the whole oligomer is given by (abcd) 3 L 3 (abcd), or alternatively, (abcd) 4 L 3 [17,18].…”

Section: Introductionmentioning

confidence: 99%

Recent New Characterizations on the Giant Extracellular Hemoglobin of Glossoscolex paulistus and Some Other Giant Hemoglobins from Different Worms

Tabak¹,

Carvalho²,

Carvalho³

et al. 2012

Stoichiometry and Research - The Importance of Quantity in Biomedicine

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 99%

Recent New Characterizations on the Giant Extracellular Hemoglobin of Glossoscolex paulistus and Some Other Giant Hemoglobins from Different Worms

Tabak¹,

Carvalho²,

Carvalho³

et al. 2012

Stoichiometry and Research - The Importance of Quantity in Biomedicine

View full text Add to dashboard Cite

“…The extracellular nature and giant size of these molecules have made them ideal systems for a number of seminal investigations into protein structure. Lumbricus erythrocruorin was the first protein ever reported to be crystallized, in 1840 (1), one of the first subjects of Svedberg's early ultracentrifugation experiments (2), and an early molecular subject of electron microscopic analysis (3).…”

mentioning

confidence: 99%

Structural hierarchy in erythrocruorin, the giant respiratory assemblage of annelids

Royer

Strand

Heel

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Many annelids, including the earthworm Lumbricus terrestris, have giant cooperative respiratory proteins (molecular masses greater than 3.5 million Da) freely dissolved in the blood, rather than packaged in cells. These complexes, termed either erythrocruorins or hemoglobins, are assembled from many copies of both hemoglobin subunits and nonhemoglobin or ''linker'' subunits. In this paper, we present the crystal structure of Lumbricus erythrocruorin at 5.5-Å resolution, which reveals a remarkable hierarchical organization of 144 oxygen-binding hemoglobin subunits and 36 nonhemoglobin linker subunits. The hemoglobin chains arrange in novel dodecameric substructures. Twelve trimeric linker complexes project triple-stranded helical coiled-coil ''spokes'' toward the center of the complex; interdigitation of these spokes appears crucial for stabilization. The resulting complex of linker chains forms a scaffold on which twelve hemoglobin dodecamers assemble. This structure specifies the unique, self-limited assemblage of a highly cooperative single molecule.

show abstract

“…HBL Hb to be investigated by ultracentrifugation [7] and by transmission electron microscopy (TEM) [8]. Although the functional respiratory properties of A. marina Hb have been well studied over many years [9][10][11][12][13][14][15][16][17][18], its structure remains poorly understood despite several electrophoretic studies [19 -241.…”

mentioning

confidence: 99%

Quaternary Structure of the Extracellular Haemoglobin of the Lugworm Arenicola marina

Zal

Green²,

Lallier

et al. 1997

European Journal of Biochemistry

View full text Add to dashboard Cite

To elucidate the quaternary structure of the extracellular haemoglobin (Hb) of the marine polychaete Arenicola marina (lugworm) it was subjected to multi-angle laser-light scattering (MALLS) and to electrospray-ionisation mass spectrometry (ESI-MS). It was also subjected to SDS/PAGE analysis for comparative purposes. MALLS analysis gave a molecular mass of 3648 % 24 kDa and a gyration radius of 11.3 rt 1.7 nm. Maximum entropy analysis of the multiply charged electrospray spectra of the native, dehaemed, reduced and carbamidomethylated Hb forms, provided its complete polypeptide chain and subunit composition. We found, in the reduced condition, eight globin chains of molecular masses 15952. Keywords: Arenicola ; haemoglobin ; quaternary structure ; multi-angle laser-light scattering; electrospray mass spectrometry.The giant extracellular haemoglobins (Hb) and chlorocruorins found in annelids [1] and vestimentiferans [2, 31 are characterised by an acidic isoelectric point and by an hexagonal symmetry in electron micrographs consisting of two superimposed hexagonal arrays of twelve spherical subunits, the hexagonal bilayer (HBL). These HBL Hb also contain a low haem and iron contents (about 67% of those observed in other Hbs) and consist of two types of chains, globin chains (~1 6 -1 8 kDa), accounting for approximately 70% of the total mass, and haem-deficient linker chains (~2 4 -2 8 kDa) necessary for the assemblage into the HBL structure [1,. The intertidal marine polychaete Arenicola marina (L.) was one of the first 60s (~3 6 0 0 kDa)

show abstract

The Molecular Weight of Erythrocruorin

Cited by 98 publications

References 2 publications

Recent New Characterizations on the Giant Extracellular Hemoglobin of Glossoscolex paulistus and Some Other Giant Hemoglobins from Different Worms

Recent New Characterizations on the Giant Extracellular Hemoglobin of Glossoscolex paulistus and Some Other Giant Hemoglobins from Different Worms

Structural hierarchy in erythrocruorin, the giant respiratory assemblage of annelids

Quaternary Structure of the Extracellular Haemoglobin of the Lugworm Arenicola marina

Contact Info

Product

Resources

About