Abstract:
:To elucidate hydroxyapatite-protein interaction, mutant human lysozymes in which the surface charge was modified by site-directed mutagenesis were used. Five mutant human lysozymes (K1A, K13A, K33A, R10A, R14A) were expressed in yeast. The chromatographic behavior of these lysozymes was studied with a HPLC hydroxyapatite column. Elution molarities of K1A and R14A mutants were greatly lowered. While Lys-13 and Arg-10 are located around Lys-1 and Arg-14, K13A and R10A mutants bound onto hydroxyapatite stronger than K1A and R14A mutants. In combination with an X-ray crystal structure of human lysozyme, it is concluded that the adsorbing site of human lysozyme is at the back of the active site and that Arg-14, Lys-1, Arg-10 and Lys-13 play important roles in binding.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Aizawa T,Koganesawa N,Kamakura A,Masaki K,Matsuura A,Nagadome H,Terada Y,Kawano K,Nitta Kdoi
10.1016/s0014-5793(97)01621-9subject
Has Abstractpub_date
1998-01-30 00:00:00pages
175-8issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(97)01621-9journal_volume
422pub_type
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