Abstract:
:A novel calcium-dependent serine proteinase (CASP) secreted from malignant hamster embryo fibroblast Ni 12C2 degrades extracellular matrix proteins. A complementary DNA encoding CASP has been isolated with the use of oligonucleotide probes synthesized based on partial amino acid sequences of CASP. The complete amino acid sequences of CASP revealed that it has a active site at the C-terminal side. Glu rich and proEGF homologous sites are found at the N-terminal site suggesting that it is structurally similar to blood coagulation factors such as IX, X and an anticoagulation factor, protein C.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kinoshita H,Sakiyama H,Tokunaga K,Imajoh-Ohmi S,Hamada Y,Isono K,Sakiyama Sdoi
10.1016/0014-5793(89)80766-5subject
Has Abstractpub_date
1989-07-03 00:00:00pages
411-5issue
2eissn
0014-5793issn
1873-3468journal_volume
250pub_type
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