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Purification, composition and Ca 2+ ‐binding properties of the monomeric protein of the S‐layer of Thermus thermophilus
Author(s) -
Faraldo Maria Luisa M.,
de Pedro Miguel A.,
Berenguer Jose
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81244-4
Subject(s) - thermus thermophilus , thermostability , chemistry , s layer , dissociation constant , biochemistry , crystallography , thermus , thermophile , enzyme , escherichia coli , receptor , gene
The S‐layer of Thermus thermophilus is apparently formed by a single protein of M r 100 000 called P100. In the cell envelope of the organism, P100 forms oligomeric complexes of exceptional thermostability in the presence of Ca 2+ . A simple and rapid method for the purification of P100 is reported. The amino acid composition of the protein was found to be comparable to that of other S‐layer proteins. Binding of Ca 2+ to P100 occurs with a dissociation constant of 50 μM apparently at 12 high‐affinity sites per P100 molecule.