Abstract
The amino acid sequence of protein Z has been determined from sequence analysis performed on fragments obtained by chemical and enzymatic degradations. The polypeptide consists of a single chain containing 396 amino acid residues (Mr 43 677). Comparison with the vitamin K-dependent plasma proteins reveals an extensive homology. The N-terminal part, containing 13 gamma-carboxyglutamic acid and one beta-hydroxyaspartic acid residue, is extensively homologous to and of similar length to the light chain of factor X. The remainder of protein Z is homologous to the serine proteases and of similar size to the heavy chain of factor Xa, but of the active site residues only aspartic acid-102 is present. Histidine-57 and serine-195 are replaced in protein Z by threonine and alanine, respectively. The physiological function of protein Z is still uncertain.
Originalsprog | Engelsk |
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Tidsskrift | FEBS Letters |
Vol/bind | 184 |
Udgave nummer | 2 |
Sider (fra-til) | 333-8 |
Antal sider | 6 |
ISSN | 1873-3468 |
DOI | |
Status | Udgivet - 20. maj 1985 |