HEMOCYANIN FROM THE AUSTRALIAN FRESHWATER CRAYFISH CHERAX-DESTRUCTOR - ELECTRON-MICROSCOPY OF NATIVE AND REASSEMBLED MOLECULES

被引:14
作者
JEFFREY, PD
机构
[1] the Department of Physical Biochemistry, John Curtin School of Medical Research, The Australian National University, The Netherlands Organization for the Advancement of Pure Research (Z.W.O.), Canberra
关键词
D O I
10.1021/bi00579a012
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Examination and measurement of electron micrographs of negatively stained hemocyanin molecules from Cherax destructor show that the predominant aggregated forms, the 16S and 24S components, are typical structures for arthropod hexamers and dodecamers, respectively. In Cherax hemocyanin the hexamers are formed from the monomeric (Mr ≃75 000) subunits, M. and M2, while the dodecamers contain in addition a dimeric (Mr ≃150 000) subunit, M3‘. Studies of the composition of solutions of the subunits M1 and M2 to which calcium ions have been added at pH 7.8 show that, under these conditions, reassembly occurs to particles in distinguishable from native hexamers. It is noteworthy that dodecamers are not seen since this confirms the previous suggestion that incorporation of the dimeric subunit in the assembly process is necessary for their formation. The results obtained from Cherax hemocyanin are related to those of previous structural studies of arthropod hemocyanins. In particular, the possible controlling role of certain specific subunits in arthropod hemocyanin oligomers containing more than one kind of subunit is illustrated with a model for the Cherax dodecamer, in which the dimeric subunit is shared between the two halves of the molecule. © 1979, American Chemical Society. All rights reserved.
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页码:2508 / 2513
页数:6
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