The characterization of the hemoglobins of the bivalve mollusc Phacoides pectinatus (Gmelin)

1. 1. The hemoglobins of the ctenidia of the bivalve mollusc Phacoides pectinatus (Gmelin), as prepared in this work, have been resolved at leas three components by means of gel-filtration and ion-exchange chromatography. The components are designated b-1, Hb-2 and Hb-3. 2. 2. The components are ele...

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Published inComparative biochemistry and physiology Vol. 15; no. 2; pp. 137,IN7,145 - 144,IN8,157
Main Author Read, K R
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 01.06.1965
Subjects
Amino Acids
Animals
Chemical Phenomena
Chemistry
Chromatography, Gel
Chromatography, Ion Exchange
Dextrans
Electrophoresis
Hemoglobins
Molecular Weight
Mollusca
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Summary:1. 1. The hemoglobins of the ctenidia of the bivalve mollusc Phacoides pectinatus (Gmelin), as prepared in this work, have been resolved at leas three components by means of gel-filtration and ion-exchange chromatography. The components are designated b-1, Hb-2 and Hb-3. 2. 2. The components are electrophoretically distinct. 3. 3. Hb-1 has a molecular weight of 14,581 computed from its amino acid composition. It is monomeric in solution. The molecule of Hb-1 contains one heme group. 4. 4. Hb-2 is probably tetrameric in concentrated solution. 5. 5. Hb-3 may aggregate into octamers or higher polymers in concentrated solution. 6. 6. In dilute solution the aggregates of both Hb-2 and Hb-3 dissociate. 7. 7. The absorption spectra of the three carbonmonoxyhemoglobins are reported. 8. 8. The amino acid composition of Hb-1 is discussed in relation to other vertebrate and invertebrate hemoglobins and in relation to evolution.
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ISSN:0010-406X
DOI:10.1016/0010-406X(65)90342-7