Limited proteolysis of the haemocyanin of the gastropod Pila leopoldvillensis. Isolation and characterization of the fragments

Limited proteolysis with trypsin and endoproteinase Glu-C of dimers of subunits of the haemocyanin of Pila leopoldvillensis revealed the presence of eight functional (dioxygen binding) units ( a- h) per subunit ( M r ≈ 435,000). Fragments a- c, d- g and ( d- h) 2 (dimer of d- h) and the dimer of fun...

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Bibliographic Details
Published in:Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 1995, Vol.110 (3), p.565-575
Main Authors: Gielens, C., Declercq, L., Préaux, G.
Format: Article
Language:English
Subjects:
Association site
Carbohydrate composition
Copper content
Functional units
Gastropod
Haemocyanin
Limited proteolysis
Marine
Mollusc
Pila leopoldvillensis
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Summary:Limited proteolysis with trypsin and endoproteinase Glu-C of dimers of subunits of the haemocyanin of Pila leopoldvillensis revealed the presence of eight functional (dioxygen binding) units ( a- h) per subunit ( M r ≈ 435,000). Fragments a- c, d- g and ( d- h) 2 (dimer of d- h) and the dimer of functional unit h ( h 2) were isolated and characterized (copper content, M r , N- and C-terminus, crossed immunoelectrophoresis, absorption and circular dichroic spectra, carbohydrate composition). Functional unit h contains the association site between the two subunits in a dimer. When compared with the average values for a functional unit it, moreover, shows a higher M r (≈65,000 vs ≈55,000) and a higher carbohydrate content (≈5.5%, w/w, vs ≈3.5%).
ISSN:1096-4959
0305-0491
1879-1107
DOI:10.1016/0305-0491(94)00175-T