FN Archimer Export Format
PT J
TI Zinc-hemocyanin binding in the hemolymph of carcinus maenas (crustacea, decapoda)
BT 
AF MARTIN, Jean-Louis
   VAN WORMHOUDT, A.
   CECCALDI, H.J.
AS 1:;2:;3:;
FF 1:;2:;3:;
TC 0
UR https://archimer.ifremer.fr/doc/1977/publication-5192.pdf
LA English
DT Article
DE ;Histoire Ifremer
AB 1. A quantitative and electrophoretic study of copper and zinc in hemolymph of the crustacea decapoda, Carcinus maenas, has been carried out. 2. Most of the copper was linked with hemocyanin.3. All copper-binding proteins are hemocyanin.4. Zinc belongs to three different compartments: more than 68% is linked with hemocyanin; about 10% is shown in the fraction containing blood cells, lipids and carotenoids; 15% is present in the hemolymph under a soluble and dialysable form. 5. Specific zinc-binding protein has not been found out in the serum of Carcinus maenas.6. Zinc linked with hemocyanin is found on high molecular weight protein fractions only. [NOT CONTROLLED OCR]
PY 1977
SO Comparative Biochemistry and Physiology
PU Pergamon Press
VL 58A
BP 193
EP 195
ID 5192
ER

EF