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HERO ID
7860101
Reference Type
Journal Article
Title
THE QUATERNARY STRUCTURE OF THE LOBSTER CARAPACE CAROTENOPROTEIN, CRUSTACYANIN - STUDIES USING CROSS-LINKING AGENTS
Author(s)
Zagalsky, PF; Mummery, RS; Eliopoulos, EE; Findlay, JBC
Year
1990
Is Peer Reviewed?
Yes
Journal
Comparative Biochemistry and Physiology - B: Comparative Biochemistry
ISSN:
0305-0491
Publisher
PERGAMON-ELSEVIER SCIENCE LTD
Location
OXFORD
Volume
97
Issue
4
Page Numbers
837-848
Language
English
DOI
10.1016/0305-0491(90)90131-C
Web of Science Id
WOS:A1990EQ43500034
Abstract
1. 1. Three bis(imidoesters) of different span (ca 9-11 Å) have been used to form intermolecular cross-links between the apoproteins of the lobster carapace carotenoprotein, α-crustacyanin. 2. 2. Dimethylpimelimidate(DMP) is the most effective of the three reagents in cross-linking the oligomeric α-crustacyanin, giving predominantly dimers between apoproteins from each of the two apoprotein classes. The native dimers, β-crustacyanins, are effectively cross-linked with this reagent. 3. 3. The stability of DMP cross-linked α-crustacyanin and of the native carotenoprotein to urea treatment and to heating have been compared. 4. 4. Reagents of longer (sulpho-N-hydroxy-succinimide ester; 18 Å) or shorter (1,5-difluoro-2,4-dinitrobenzene; 5 Å) spans than the bis(imidoesters) are similarly able to form cross-linked dimers with the crustacyanins, but less effectively under the conditions of the reactions. 5. 5. The results are discussed in relation to the previously presented putative structure of β-crustacyanin (Keen et al. 1990b. Eur. J. Biochem. (submitted); Zagalsky et al., 1990. Comp. Biochem. Physiol. 97B, 1-18) and to an alternative subunit interface arrangement of the apoproteins for the dimer. © 1990.
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