ISSN:
1435-5604
Schlagwort(e):
Key words: osteocalcin
;
cathepsin B
;
cathepsin L
;
papain
;
calcium-binding capability
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Medizin
Notizen:
Abstract: Rat osteocalcin was subjected to proteolysis by cathepsins B and L at acid pH in vitro. Short fragments of fewer than 8 amino acids were liberated from both the NH2- and COOH-termini of the molecule, but the midportion, composed of antiparallel α-helical domains, was resistant to proteolysis. Intact rat osteocalcin bound 10 Ca2+/mol protein at pH 7.5 and the binding decreased to half that amount at pH 5.0, while the midportion fragment (Ala8-Lys43) bound 4–5 Ca2+/mol protein at both pH 5.0 and 7.5. When COOH-terminal-truncated rat osteocalcin (Tyr1-Lys43) was prepared with lysyl-endopeptidase, it showed nearly the same Ca2+ binding as that of the intact molecule. Our results suggest that proteolytic processing of the terminal sequence of osteocalcin alters its intrinsic Ca2+-binding capacity and that its NH2-terminal sequence is probably involved.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/s007740050029
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