Primary structure of a constituent polypeptide chain of the chlorocruorin from Sabellastarte indica

Suzuki, Tomohiko; Hirao, Yuriko; Vinogradov, Serge N.

doi:10.1016/0167-4838(95)00147-m

Cited by 6 publications

(6 citation statements)

References 11 publications

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“…(from Japanese sea vents) [76] Ridgeia piscesae, Oasisia alvinae, Tevnia jerichonana and Lamellibrachia nov sp. (from Mediterranean sea vents) [20], the pogonophoran Oligobrachia mashikoi [77], as well as surface species not associated with bacterial symbionts, such as the polychaetes Sabella spallanzanii [78], Sabellastarte indica [79], Arenicola marina [80], Alvinella pompejana and Scoloplos armiger (Bailly et al unpublished data). Given the demonstration of the sulfide-binding function of the hemoglobins from Riftia pachyptila, the vestimentiferans Lamellibrachia luymesi and Seepiophila jonesi [83] and the polychaete Arenicola marina [82], it is likely that the hemoglobins of all the foregoing species have the ability to bind sulfide via their free cysteine residues.…”

Section: Free Cysteine Residues In Other Annelids Inhabiting Sulfide-mentioning

confidence: 96%

The sulfide binding function of annelid hemoglobins: relic of an old biosystem?

Bailly

Vinogradov

2005

Journal of Inorganic Biochemistry

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Section: Free Cysteine Residues In Other Annelids Inhabiting Sulfide-mentioning

confidence: 96%

The sulfide binding function of annelid hemoglobins: relic of an old biosystem?

Bailly

Vinogradov

2005

Journal of Inorganic Biochemistry

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“…Sequence Alignment and Characterization-To characterize the primary structure of the Sabella globin chains, we have aligned them with the annelid, pogonophoran, and vestimentiferan globin sequences available in our data base including a globin chain from the Chl of S. indica and globin references (17)(18)(19). A representative selection of this alignment is presented in Fig.…”

Section: Primary Structure Of Sabella Globins and Linkersmentioning

confidence: 99%

“…In contrast to annelid Hbs, in which a wealth of sequence information of globin chains is available, only a single primary structure of a Chl globin chain has been published (17). Globin chain E of Sabellastarte indica shows 27-49% sequence identity with the annelid globin chains.…”

mentioning

confidence: 99%

The Primary Structure of Globin and Linker Chains from the Chlorocruorin of the Polychaete Sabella spallanzanii

Pallavicini¹,

Negrisolo²,

Barbato³

et al. 2001

Journal of Biological Chemistry

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Annelid hemoglobins are organized in a very complex supramolecular network of interacting polypeptides, the structure of which is still not wholly resolved. We have separated by two-dimensional electrophoresis the 4-MDa chlorocruorin of Sabella spallanzanii and identified its components by amino-terminal sequencing. This work reveals a high rate of heterogeneity of constituent chains in a single animal as well as in the Sabella population. Using a cDNA library prepared from the hematopoietic tissue of this worm, we have isolated and fully sequenced most globin and linker cDNAs. The primary structure features of these polypeptides have been characterized by comparison with model globin and linker sequences.

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“…Vestimentifera Riftia pachyptila: A1 (CAD29154), A2 (P80592), B1a (CAD29156), B1b (CAD23157), B1c (CAD29158), B2 (CAD29159). Vestimentifera Lamellibrachia sp: the amino acid sequences of each globin chains (A1, A2, B1, B2) were obtained from the reference (Suzuki et al, 1995). Annelida Lumbricus terrestris: A1 (B28151), A2 (A29134), B1 (C28151), B2 (A28151).…”

Section: Purification and Characterization Of The O Mashikoi Giant Hmentioning

confidence: 99%

“…The amino acid sequences of the extracellular giant hemoglobins from Pogonophora, Vestimentifera, Annelida and Mollusca, human hemoglobin and myoglobin were obtained from the Entrez Protein program (http://www.ncbi.nlm.nih.gov/entrez/index.html) and from the reference (Suzuki et al ., 1995). The structures of hemoglobins were observed with MMDB and Entrez Structure program (http:// www.ncbi.nih.gov/Structure/).…”

Section: Informative Search Multiple Alignment and Phylogenetic Analmentioning

confidence: 99%

Purification, Characterization and Sequence Analyses of the Extracellular Giant Hemoglobin from Oligobrachia mashikoi

et al. 2005

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-We purified an extracellular hemoglobin with the molecular mass of ca. 440 kDa from the whole homogenates of Oligobrachia mashikoi (phylum Pogonophora) by a one-step gel-filtration. The preparation was pure to be crystallized. The P 50 values of the hemoglobin and the fresh blood prepared from O. mashikoi were about 0.82 Torr and 0.9 Torr, respectively, which were much lower than the P 50 value of human hemoglobin. However, the n values of the hemoglobin and the blood were about 1.2 and 1.1, respectively.Using the improved tricine SDS-PAGE, we could separate O. mashikoi hemoglobin into four kinds of the globin chains, A1, A2, B1 and B2, and succeeded for the first time in cloning and sequencing of the complete cDNA encoding B1 globin gene, in addition to A1, A2 and B2 globin genes in full length. We found that all globin genes have the extracellular signal sequences in each molecule and the distal His of the B1 globin chain is replaced to Gln. Finally, we constructed phylogenetic trees of the hemoglobins from Pogonophora, Vestimentifera and Annelida.

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Primary structure of a constituent polypeptide chain of the chlorocruorin from Sabellastarte indica

Cited by 6 publications

References 11 publications

The sulfide binding function of annelid hemoglobins: relic of an old biosystem?

The sulfide binding function of annelid hemoglobins: relic of an old biosystem?

The Primary Structure of Globin and Linker Chains from the Chlorocruorin of the Polychaete Sabella spallanzanii

Purification, Characterization and Sequence Analyses of the Extracellular Giant Hemoglobin from Oligobrachia mashikoi

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