Abstract：
:Sequences of 40 very diverse representatives of the alpha-crystallin-small heat-shock protein (alpha-Hsp) superfamily are compared. Their characteristic C-terminal 'alpha-crystallin domain' of 80-100 residues contains short consensus sequences that are highly conserved from prokaryotes to eukaryotes. There are, in addition, some positions that clearly distinguish animal from non-animal alpha-Hsps. The alpha-crystallin domain is predicted to consist of two hydrophobic beta-sheet motifs, separated by a hydrophilic region which is variable in length. Combination of a conserved alpha-crystallin domain with a variable N-terminal domain and C-terminal extension probably modulates the properties of the various alpha-Hsps as stress-protective and structural oligomeric proteins. Phylogeny reconstruction indicates that multiple alpha-Hsps were already present in the last common ancestor of pro- and eukaryotes. It is suggested that during eukaryote evolution, animal and non-animal alpha-Hsps originated from different ancestral gene copies. Repeated gene duplications gave rise to the multiple alpha-Hsps present in most organisms.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
de Jong WW,Caspers GJ,Leunissen JAdoi
10.1016/s0141-8130(98)00013-0subject
Has Abstractpub_date
1998-05-01 00:00:00pages
151-62issue
3-4eissn
0141-8130issn
1879-0003pii
S0141-8130(98)00013-0journal_volume
22pub_type
杂志文章,评审abstract：:The equilibrium isotherms and adsorption kinetics of lysozyme (LZ) on epichlorohydrin (Epi) cross-linked alginate-guar gum (Alg-GG) matrix were studied. Adsorption kinetics followed a pseudo-first-order model while the equilibrium isotherm could be represented by the Freundlich equation. The maximal amount of LZ adsor...
journal_title：International journal of biological macromolecules
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journal_title：International journal of biological macromolecules
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journal_title：International journal of biological macromolecules
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