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Titlebook: Invertebrate Oxygen Carriers; Bernt Linzen Conference proceedings 1986 Springer-Verlag Berlin Heidelberg 1986 Calcium.Mollusca.Peptide.X-r

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發(fā)表于 2025-3-21 17:17:54 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Invertebrate Oxygen Carriers
編輯Bernt Linzen
視頻videohttp://file.papertrans.cn/475/474732/474732.mp4
圖書封面Titlebook: Invertebrate Oxygen Carriers;  Bernt Linzen Conference proceedings 1986 Springer-Verlag Berlin Heidelberg 1986 Calcium.Mollusca.Peptide.X-r
出版日期Conference proceedings 1986
關(guān)鍵詞Calcium; Mollusca; Peptide; X-ray; amino acid; cells; electron microscopy; evolution; kinetics; microscopy; mo
版次1
doihttps://doi.org/10.1007/978-3-642-71481-8
isbn_softcover978-3-540-16943-7
isbn_ebook978-3-642-71481-8
copyrightSpringer-Verlag Berlin Heidelberg 1986
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The Dissociation of the Extracellular Hemoglobin of Lumbricus Terrestris: A Model of Its Subunit Stride chains: I through IV (M. 16–19 kDa) and V (M. 31kDa) and VI (M. 37kDa) (7). SDS PAGE of the unreduced hemoglobin shows that it consists of four subunits: M (chain I), D1 (chain V), D2 (chain VI) and subunit T, a disulfide-bonded trimer of chains II, III and IV (4–7). Figure 1 shows the relationship between the two sets of subunits.
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Oxygen Equilibria of Whole Molecules, Isolated Subunits and the Subunit Trimer of Hemoglobin from ,olated subunits, trimer, and the reconstructed 4 chain product show that the trimer retains both the Bohr and the Ca. effects. Addition of the 4th chain to the trimer results in regeneration of much of the cooperativity present in the native molecule.
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Quaternary Structure and Modulation of Function in Earthworm Erythrocruorincentral cavity, each layer consisting of six subunits; in turn the 1/12 subunits are formed by three or four lower molecular weight ones (1,2). However, the detailed arrangement of the constituent polypeptide chains in the subunits appearing in the electron microscope is still elusive.
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Homage to René LontieIt is a great pleasure for me to pay homage on behalf of the hemocyanin community to René Lontie on the occasion of his 65th birthday, for his scientific career dedicated to the study of proteins, in particular of the nature and function of hemocyanins.
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978-3-540-16943-7Springer-Verlag Berlin Heidelberg 1986
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