Electrospray ionization mass spectrometric composition of the 400 kDa hemoglobin from the pogonophoran Oligobrachia mashikoi and the primary structures of three major globin chains.

Yuasa, H J; Green, B N; Takagi, T; Suzuki, N; Vinogradov, S N; Suzuki, T

Yuasa, H J; Green, B N; Takagi, T; Suzuki, N; Vinogradov, S N; Suzuki, T.

Affiliation

Yuasa HJ; Department of Biology, Faculty of Science, Kochi University, Japan.

Biochim Biophys Acta ; 1296(2): 235-44, 1996 Sep 05.

Article in En | MEDLINE | ID: mdl-8814231

Subject(s)

Hemoglobins/chemistry; Invertebrates/chemistry; Mass Spectrometry; Amino Acid Sequence; Animals; Base Sequence; Chromatography, Gel; Evolution, Molecular; Humans; Molecular Sequence Data; Molecular Weight; Phylogeny; Protein Conformation; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity

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Collection: 01-internacional Database: MEDLINE Main subject: Mass Spectrometry / Hemoglobins / Invertebrates Limits: Animals / Humans Language: En Journal: Biochim Biophys Acta Year: 1996 Document type: Article Affiliation country: Japan Country of publication: Netherlands

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