Premium
Properties of the extracellular calcium binding module of the proteoglycan testican
Author(s) -
Kohfeldt Eddie,
Maurer Patrik,
Vannahme Christian,
Timpl Rupert
Publication year - 1997
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/s0014-5793(97)01070-3
Subject(s) - extracellular , calcium , chemistry , recombinant dna , proteoglycan , biophysics , biochemistry , calcium binding protein , plasma protein binding , microbiology and biotechnology , biology , extracellular matrix , gene , organic chemistry
The extracellular calcium‐binding (EC) module of human testican (115 residues) was obtained in native form by recombinant production in mammalian cell culture and thus shown to represent an independently folding domain. This module showed a large loss in α‐helix upon calcium depletion. Apparently only one of the two EF hands binds calcium, with a moderate affinity ( K d =68 μM) about 100‐fold lower than in the homologous BM‐40 protein. No clear evidence was obtained for collagen binding, indicating that EC modules found in different proteins may not share similar functions.