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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Højrup P,Jensen MS,Petersen TEdoi
10.1016/0014-5793(85)80633-5subject
Has Abstractpub_date
1985-05-20 00:00:00pages
333-8issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(85)80633-5journal_volume
184pub_type
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